Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biochem > Final > Flashcards

Final Flashcards

1
Q

what are the fundamental units of life

A

cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what do cells use overall in organisms

A

relatively small set of carbon based metabolites to create polymeric machines, suprmolecular structures and information repositories

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what state do living organisms exist in

A

dynamic steady state, never at equilibrium with their surroundings

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

why cant organisms be in equilibirum with their surroundings

A

we would be dead

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what do cells have the capacity for

A

precise self replication and self assembly using chemical information stored in gemoe

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

do living organisms change overtime

A

yes by gradual evolution

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

size difference of a bacteria cell and an animal cell

A

bacteria is much smaller, animal usually 10x larger

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Angstrum

A

1 x 10^-10

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

out side difference or similarties of animal and bacteria cell

A

both have plasma membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

inside differences and similarities of animal and plant cell

A

both have cytoplasm
animal cells are membrane bound organelles (bacteria is not)
genetic info held in the nucleus of animals
genetic info floats in bacteria
both have ribosomes responsible for reading mRNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

quote about ecoli and elephant

A

what is true of ecoli is true of the elephant

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

the domains of life

A

bacteria, archea, and eukarya

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what can classify living things

A

their energy and their carbon source

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

what are our main sources of energy

A

organic chemicals

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what is the light microscope

A

wavelengths of visible length (400-750 nm
you can see the cell with this but cant tell info about the small things inside the cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

size of a typical cell

A

10s of um
usually 20um-20,000nm

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

size of plasma membrane

A

50A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

size of DNA

A

18A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

size of nucleotides

A

10A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

size of amino acids

A

3-5A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Size of protein

A

5A but could be as large as 10A i things are sticking out

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

size of C-C bond

A

1.5A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

size of C-H

A

1.1 A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

what makes up most of the cell

A

water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

what else makes up a cell

A

proteins
RNA
polysaccahirdes
lipids
monomeric subunits
DNA
inorganic ions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

valence electrons in
H
C
N
P
O
S
Halogens

A

1H
4C
5N
5P
6O
6S
7Halogens

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

LOOK AT FUNCTIONAL GROUPS

A

FUNCTIONAL GROUPS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

what are biological molecules combinations of

A

functional groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

what makes up a double bond

A

sigma bond + pi bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

what is the stronger bond in a double bond

A

pi bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

diasteriomer

A

not a mirror image

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

enantiomer

A

mirror immage

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

why is metabolic energy spent

A

to do cellular work

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

how does entropy change in a system

A

entropy of the system and surroundings increase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

where is potential energy

A

nutrients in environemnt (complex molecules like sugars and fats)
sunlight for plants

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

what are the energy transductions that accomplish work

A

chemical transformations within cells
heat
metabolism
polymerition

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

what are the chemical transformations within cells

A

cellular work:
chemcial synthesis
mechanical work
osmotic and electrical gradients
light production
genetic information trasnfer

bascially take potential enery and convert it to do work, work will synthesize new molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

does heat cause more or less disorder

A

more
cells produce lots of excess eat as a side product, keeps our body at a warm temp
disorder goes into environment by heating up

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

what does metabolism do

A

produces compounds simpler than the initial fuel molecules

breaking down sugars and fats we breathe out small molecules like CO2 which are more disordered

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

what is the polymerization that happens in cells

A

simple compounds polymerize to form information rich macromolecules, DNA, RNA and protiens

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

what is the main energy currency

A

ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

how to break ATP

A

hydrolysis, water across the bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

ATP equation

A

H2O + ATP (4-) –> ADP (3-) + Pi(2-) + H+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

what happens when you phosphorylate glucose

A

means you add them together and the sum is favorable

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

anabolic

A

builds, what it is using

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

catabolic

A

break down

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

basic idea of metabolism

A

organisms take in energy and break down into simple molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

what allows for evolution

A

changes in heredity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

how much change is needed for a new mutation

A

1 base change can change the amino acid which changes its function

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

what did life likely evolve from

A

RNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

what do we think ancestral cells did to allow for the genetic diversity we have today

A

ancestral cell engulfed mitocondria leading to more complex eukaryotic cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

what is water

A

a small bend molecular with polar bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

partial charges on water

A

partial positives on the 2 hydorgens and partial negatives on the 2 sets of oxygen electrongs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

what can water molecules do

A

ionize

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

what does ionization allow for in water

A

allows protons to hop in aqueous solution,

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

what explains the high ionic mobility of the H+ in solution

A

ionization

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

pH=

A

-log[H+]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

pOH=

A

-log[OH-]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

pH+pOH=

A

14

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

PRACTICE PH AND POH EQUATIONS

A

EQUATIONS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

weak acid

A

acid that doesnt completely dissociate in a solution

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

conjugate base

A

removal of a proton from an atom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

monoprotic acid

A

can only donate one proton

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

monoprotic acid examples

A

acetic acid and ammoniun ion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

diprotic acid

A

have 2 acidic hydrogen atoms, yields 2 hydrogen ions per acid molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
66
Q

examples of diprotic acids

A

carbonic acid, bicarbonate, glycine carboxyl, glycine amino

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
67
Q

triprotic acid

A

has 3 acidic hydrogen atoms

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
68
Q

triprotic acid examples

A

phosphoric acid, dihydirgen phosphate, monohydrogen phosphate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
69
Q

what is a buffer

A

mixture of a weak acid and their conjugate base allowing for pH consistance

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
70
Q

when do you do a weak acid calculation

A

when no buffer is present

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
71
Q

Henderson Hasselbalch equation

A

pH=pka + log[A-]/[HA]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
72
Q

main buffering system in cells

A

phosphate system

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
73
Q

main buffering system in blood

A

bicarbonate system

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
74
Q

what happens to the buffering system in people with diabetes

A

body will oxidize fat causing your body to be more acidic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
75
Q

Special traits of water

A

strong intramolecular forces (hydrogen bonds)
High melting and boiling points
high heat of vaporization

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
76
Q

how many hydrogen bonds can water form

A

4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
77
Q

how many hydrogen bond acceptors in water

A

2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
78
Q

how many hydrogen bond donors in water

A

2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
79
Q

ice water males how many hydirgen bonds

A

4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
80
Q

liquid water makes how many hydrogen bonds

A

3.4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
81
Q

why are the hydrogen bonds in liquid water less than it solid water

A

the moelcules of water can be closer in liquid form so it increases the density

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
82
Q

what has a lower density ice or liquid water

A

ice, why it floats

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
83
Q

why do snowflakes have hexagonal symmetry

A

increase in entropy drives the melting of ice and the evaporation of water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
84
Q

what are the hydrogen acceptors

A

O or N or F (rare)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
85
Q

hydirgen donors

A

water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
86
Q

characteristic of a hydrogen donor

A

electronegative atom

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
87
Q

characterisitic of a hydorgen acceptor

A

has a lone pair

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
88
Q

what types of hydrogen bonds are stronger

A

shorter and straighter ones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
89
Q

what is the solubility of salts in water driven by

A

an increase in entropy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
90
Q

what is more soluble in water salts or less polar solvents

A

salts

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
91
Q

increase in entropy

A

disorder

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
92
Q

what is the physical reason why salt is soluble in water

A

the water is more ordered but is outcompeted by the sakt

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
93
Q

what state does oxygen have the most freedom in

A

gas phase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
94
Q

does a high or low temp favor the gas phase of water

A

high

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
95
Q

how does the temp of oceans and ponds affect water and oxygen content

A

high temps favor the gas phase which will decrease the O2 content affecting the wildlife in oceans and ponds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
96
Q

hydrophobic

A

doesnt like water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
97
Q

hydrophillic

A

likes water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
98
Q

what type of interactions bind enzyme with substrate

A

noncovalent

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
99
Q

when are water molecules displaced

A

when substrate binds to enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
100
Q

are non covalent interactions strong or weak

A

weak

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
101
Q

what is osmotic pressure

A

force necessary to resist water movement, there is a semipermeable barrier that H2O moves through but solvent does not

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
102
Q

in a more concentrated solution will water move in or out?

A

in

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
103
Q

how many amino acids are there

A

20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
104
Q

what joins amino acids together

A

peptide bonds or amide linkages

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
105
Q

proteins are separated based on what?

A

differences in their chemical and functional properties

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
106
Q

what are the building blocks of proteins

A

amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
107
Q

zwitter ion

A

in pH range of 3-10, neutral because one is protonated and one is not

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
108
Q

what orientation are amino acids in nature

A

L

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
109
Q

what is the orientation proteins are built

A

N –> C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
110
Q

what is an amino acid residue

A

lost H2O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
111
Q

quality of the peptide backbone

A

flexible

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
112
Q

N-Ca bond

A

Phi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
113
Q

Ca-C bond

A

psi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
114
Q

C-N

A

omega

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
115
Q

dihedral angle

A

angle between planes formed by the backbone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
116
Q

pKa of the carboxyl end

A

2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
117
Q

pka of amino end

A

9

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
118
Q

what is the simplest amino acid

A

glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
119
Q

pI

A

pH when charge on molecule is zero –> in between buffering zones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
120
Q

glycine

A

G

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
121
Q

alanine

A

A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
122
Q

proline

A

P

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
123
Q

valine

A

V

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
124
Q

leucine

A

L

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
125
Q

isoleucine

A

I

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
126
Q

methionine

A

M

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
127
Q

Phenylalanine

A

F

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
128
Q

Tyrosine

A

Y

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
129
Q

Tryptophan

A

W

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
130
Q

Serine

A

S

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
131
Q

Threonine

A

T

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
132
Q

Cysteine

A

C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
133
Q

Asparagine

A

N

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
134
Q

Glutamine

A

Q

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
135
Q

Lysine

A

K

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
136
Q

Histidine

A

H

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
137
Q

Arginine

A

R

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
138
Q

Aspartate

A

D

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
139
Q

Glutamte

A

E

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
140
Q

pKa of tyrosine

A

10.07

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
141
Q

pKa of cysteine

A

8.18

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
142
Q

pKa of lysine

A

10.53

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
143
Q

pKa of histidine

A

6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
144
Q

pKa of arginine

A

12.48

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
145
Q

pKa of aspartate

A

3.65

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
146
Q

pKa of glutamate

A

4.25

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
147
Q

negative hydropathy number

A

rather be in H2O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
148
Q

positive hydropathy number

A

wants to be in hydrophobic area

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
149
Q

how can amino acids be modified

A

methylation and acetylated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
150
Q

estimate molecular weight of a protein

A

residues x 110 Da

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
151
Q

what is used for protein purification

A

chromatography columns that use an aqueous buffer as the mobile phase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
152
Q

what method seperates proteins based on charge

A

ion exchnage chromatography

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
153
Q

cation exchange

A

cations will stick, must stick to something negative

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
154
Q

anion exchange

A

anions stick, resin is positice

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
155
Q

what do you add if cations are stuck to the column

A

salt

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
156
Q

what do you do to a protein with lots of positive charge

A

change pH increase so its no longer negative and wont stick

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
157
Q

what method seperates protein based on size

A

size exclusion chromatography

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
158
Q

how does size exclusion chromatography work

A

large ones move quick around the porous beads, small ones get stuck in the beads as they move through

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
159
Q

negative to size exclusion chromatography

A

it must be run slow, if it runs too fast by adding concentration but that will increase pressure which can crush/break the beads

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
160
Q

What type of protein separation is based on tags

A

affinity chromatography

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
161
Q

common tags in affinity chromatography

A

GST
His Tag
ATP-binding domaiin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
162
Q

how do proteins move in and SDS gel

A

unfolded proteins, small ones move further and large ones dont move as far

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
163
Q

how does isoelectric focusing work

A

inject protein samples with pH gradient, inject the rpteon we are looking for with neutral charge, separate by sizen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
164
Q

what is needed for mass spec

A

small sample sizes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
165
Q

solid phase protein synthesis

A

chemically from c terminus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
166
Q

steps for solid phase protein synthesis

A
  1. link first amino acid at c term
  2. need a protecting group (so right part of the backbone reacts)
  3. F molecule linked to N terminus as protecting group
  4. remove protecting group
  5. add next amino acid with protecting group
  6. remove protecting group
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
167
Q

[]

A

always whatever is within these brackets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
168
Q

{}

A

everything but whats in these brackets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
169
Q

visual representation of a protein sequence

A

sequence logo

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
170
Q

what is the pauling scale

A

concept of electrons being shared

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
171
Q

concept of x ray crystallography

A

forms cyrtials from x rays, best data from this method

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
172
Q

what is an ideal methods for determining the protein structure of smaller proteins

A

2D NMR

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
173
Q

what is a good method for determining protein structure in large proteins

A

cryo electron microscopy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
174
Q

down side to cryo electrong microscopy

A

poorer resolution, gives rough approximate shape, not exact

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
175
Q

what types of proteins do not want to form crystals

A

nonpolar, hydrophobic, membrane proteins
big floppy ones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
176
Q

how long does protein NMR take

A

6 months

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
177
Q

levels of protein structure

A

primary, secondary, tertiary, quaternary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
178
Q

primary protein strucutre

A

amino acid residues connected via covalent bonds (peptide bonds) and disulfide bridges

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
179
Q

secondary protein structure

A

common protein folding structure held together by hydrogen bonds between backbone functional groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
180
Q

tertiary protein structure

A

folded 3D structure of single chain, H bonds and other weak interactions between backbone and side chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
181
Q

quaternary structure

A

final folded structure with multiple chains (if applicable)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
182
Q

orientation of a peptide bond in a protein

A

usually trans, no free rotation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
183
Q

alpha helix protein structure level

A

secondary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
184
Q

what is an alpha helix held together by

A

hydrogen bonds between functional groups on the backbone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
185
Q

rise per amino acid

A

1.5A/amino acid residue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
186
Q

what is the orientation of hydrogen bonds in an alpha helix

A

parallel to the axis of the helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
187
Q

typical length of a hydrogen bond

A

2.8-3.1 A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
188
Q

what is stronger a shorter or a longer hydrogen bond

A

shrter

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
189
Q

which residues favor alpha helix formation

A

ala
arg
leu
glu
meth
iso

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
190
Q

where do complementary residues sit in an alpha helix

A

at the i, i+3 or i+4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
191
Q

residues that don’t fit with an alpha helix

A

glycine
proline

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
192
Q

why is glycine bad for an alpha helix

A

too flexible

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
193
Q

why is proline bad for for an alpha helix

A

too rigid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
194
Q

what is the N terminus in an aloha helix stabilized by

A

more negative residues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
195
Q

what is the c terminus of an alpha helix stabilized by

A

more positive residues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
196
Q

what level of protein strucutre is a b-sheet

A

secondary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
197
Q

what is the length of a antiparallel beta sheet per amino acid

A

3.5A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
198
Q

what is the length of a parallel beta sheet per amino acid

A

3.25 A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
199
Q

types of hydorgen bonds in an antiparallel b sheet vs a parallel b sheet

A

parallel has bent hydorgen bodns
antiparallel has stronger more stable hydirgen bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
200
Q

minimum number of strands for a b sheet

A

2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
201
Q

globular protein

A

discrete unit mixture of secondary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
202
Q

fiberous protein

A

structural role, forms long fibers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
203
Q

examples of fibrous proteins

A

alpha keratin (lots of alpha helices)
silk (beta sheets in layers)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
204
Q

do antiparallel sheets have tight or wide turns ?

A

tight

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
205
Q

smallest turn for a beta sheet

A

4 amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
206
Q

how is a beta sheet with 4 residues held together

A

by a hydrogen bond between the 1st and 4th residue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
207
Q

type 1 turn of a beta sheet

A

residue #2 is a proline in cys conformation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
208
Q

type 2 turn of a beta sheet

A

3 is a glycine which can rotate easily

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
209
Q

what is more common a type 1 or type 2 turn

A

type 1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
210
Q

what is CD spectroscopy

A

peptide will absorb left and right plan polarized light different to measure secondary protein structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
211
Q

alpha keratin

A

2 alpha helices wrapped around each other
very strong

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
212
Q

examples of alpha keratin

A

hair, skin, nails, horns, claws, wool

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
213
Q

what amino acids are found in keratin

A

ala, val, leu, iso, met, phe, cys

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
214
Q

which hand is alpha keratin

A

2 left handed helices wrapped to make it right handed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
215
Q

steps for hair straightening

A

reduce, curl, oxidize

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
216
Q

how does hair straightening work

A

chemically reorganize bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
217
Q

collagen formation

A

3 left handed helices wrapped togehter to become right handed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
218
Q

the amino acids in collagen

A

gly
pro
1,4 hydroxylproline

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
219
Q

what is needed to make hydroxyproline

A

vitamin c

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
220
Q

where is the proline and hydroxyproline found in collagen

A

packed on the outside

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
221
Q

where is the glycine found in collagen

A

packed into the middle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
222
Q

what is a special characteristics of collagen

A

cross lining cys residues which have more strength

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
223
Q

what is silk (fibroin) made up of

A

layers of anti-parallel beta sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
224
Q

characteristics of silk

A

not stretchy, soft, smooth, flexivle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
225
Q

amino acids in silk

A

ala
gly

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
226
Q

what type of linking is there in silk

A

no cross linking

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
227
Q

where is myoglobin found and what does it do

A

in muscles, holds oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
228
Q

even if we back all the atoms togehter in myoglobin and similar proteins what percent will be occupied

A

75%
25% empty space (not enough room to put anything in that space)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
229
Q

will beta sheets always be fully flat

A

never

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
230
Q

characterisitcs of folded globular proteins

A

hydrophobic effect favors 2 layers
b and a segemtns are often separate
N-C term folding
no crossover and right handed connection
favors twisted beta sheets

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
231
Q

motif

A

repeats over and over again
B-a-B loops
recognizes strucutre with 2 or more secondary strucutre and their connection

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
232
Q

a/b barrel

A

alternates back an d forth

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
233
Q

what does a higher score mean when mapping proteins

A

disorder

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
234
Q

domain

A

recognizable, independently stable

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
235
Q

fucntions of domains

A

catalytic or regulatory

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
236
Q

what does it mean if amino acids are close together in primary sequence

A

they are also close in 3D space

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
237
Q

topology diagrams

A

illustrate the secondary structure and connections, done to scale, nut cant see L vs R or the overall shape

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
238
Q

what must quaternary strucutre have

A

multiple chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
239
Q

hemoglobin strucutre

A

2 alpha chains
2 beta chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
240
Q

homo vs hetero

A

same peptides vs
different subunits

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
241
Q

why cant quanternary srucutre be mirror images

A

bc we dont have D amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
242
Q

ways to monitor protein unfolding

A

CD spectroscopy
Monitoring W flourescence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
243
Q

what does it mean to monitor W flouresence

A

very sensitive to environment, often W inside and not exposed to water which can be seen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
244
Q

what happens to an unfolded protein

A

it will aggregate so it needs proteins to get it back to its shape

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
245
Q

ways to unfold a protein

A

heat
adjust pH
add chemcials

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
246
Q

what does adding heat do to unfold a protein

A

breaks disulfide linkages adds a reducing agent

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
247
Q

what chemicals can be added to unfold a protein

A

urea, guandium, hydrochloride

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
248
Q

how to monitor protein folding

A

melting temp

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
249
Q

what is the protein melting temp

A

protein has a certain tolerance to temp before it unfolds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
250
Q

examples of chaperones that assist in folding

A

heat shock proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
251
Q

why do heat shock proteins form

A

cells stressed by heat and it creates more chaperone prtoeins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
252
Q

what can happen when proteins aggregate

A

can form large fibrils, mainly happens with extracellular proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
253
Q

how to avoid fibrils from forming

A

degrade the protein right away by sending it to the proteosome so the protease can chope it up and destory it

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
254
Q

how many alpha helicies are in myoglobin

A

8

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
255
Q

what type of fold forms in myoglobin

A

globin fold

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
256
Q

what is deep in the core of myoglobin

A

heme group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
257
Q

what does the heme group in the myoglobin prevent

A

oxidation of Fe2+ to Fe3+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
258
Q

is myoglobin conjugated or unconjugated

A

conjugated

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
259
Q

prosthetic group in myoglobin

A

heme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
260
Q

ligand for myoglobin

A

oxyegn gas, O2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
261
Q

what makes up the heme in myoglobin

A

porphyrin ring and iron

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
262
Q

where is the iron held in myoglobin

A

in the perofrin ring

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
263
Q

how many connection are there to the iron in the heme group

A

4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
264
Q

how many connections does iron like to have

A

likes to be octahedral so there are 2 open spaces

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
265
Q

what specifically connects the iron

A

proximal his residue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
266
Q

what can take up the 6th spot in the iron

A

pick up an O

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
267
Q

kd

A

concentration of ligand needed for 50% of binding sites to be occupied

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
268
Q

units for Kd

A

molar

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
269
Q

do we want a higher or lower kd for good binding to protein

A

lower

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
270
Q

what affects how well o2 can bind

A

influence of a protein

271
Q

how much needs to be conserved for it to still share a strucutre fold

A

only 1/4

272
Q

what does hemoglobin do

A

oxyegn carrier

273
Q

how much a RBC does hemoglobin take up

A

34%

274
Q

what states can hemogobin change to

A

t or r

275
Q

when is the T state preferred

A

at low Oxygen concentration

276
Q

when is the R state preferred

A

at high Oxygen concentration

277
Q

which state favors binding oxyegn

A

R

278
Q

when does hemoglobin switch from R to T states

A

changes to R in the lungs to T in the tissues

279
Q

hemoglobin is protonated when

A

at a low pH

280
Q

when protonated what does the His 146 do

A

Makes a salt bridge to aspardic acid 94
makes an ion pair to Asp94 which stabilizes the T state

281
Q

what does the CO2 do when on hemoglobin

A

it is carried by it and will covalently attach to the N terminus releasing more H+ ions

282
Q

whcih state likes to drop of oxygen and i what environment

A

T state likes to drop off oxygen
more acidic = more oxygen delivered

283
Q

what else regulates oxygen binding to hemoglobin

A

BPG

284
Q

more CO2 means

A

more O2 needed

285
Q

what is causes by a single amino acid mutation

A

sickle cell anemia

286
Q

what is the mutation in sickle cell anemia

A

beta chain has a EV6 mutation

287
Q

what is an EV6 mutation

A

glutamic acid changes to valine

288
Q

what happens at the EV6 mutation

A

allows hemoglobin to polarize make longer strands, make RBCs into rough elongated shapes, usually RBCs need o be round so they can travel through veins

289
Q

what can the EV6 be helpful with

A

provides protection against malaria

290
Q

what is different about the hemoglobin that fetuses make

A

it is higher affinity for O2 and uses the O2 in moms blood, after birth they turn off fetal version and turn on human version

291
Q

what are most enzymes

A

proteins

292
Q

what is the main function of enzymes

A

lower the activation barrier to allow system to come o equilibrium faster

293
Q

what is a spontaneous delta G

A

negative

294
Q

what do activation barriers do

A

slow down a reaction

295
Q

at what temps do enzymes typically function

A

low temps around 37 degrees C

296
Q

how fast do enzymes work

A

on the order of us

297
Q

do enzymes produce a lot of side products

A

no very few

298
Q

what are enzyme cofactors

A

usually ions, not an amino acid residue but involved in function of enzyme

299
Q

similar to enzyme cofactors

A

coenzyme

300
Q

what is a coenzyme

A

not an ion so some small organic molecule involved in function of an enzyme

301
Q

what do enzymes do to lower the activation barrier

A

speed up the rx. 10^5-10^7x

302
Q

what do covalent bonds in enzymes do

A

transient so they are temporary bonds that provide an alternative, lower energy reaction pathway

303
Q

what does acid base-catalysis mean

A

acid donates H+, base accepts H+

304
Q

what do noncovalent interactions in enzymes do

A

form an ES complex, has weak interactions between enzyme and substrate to stabilize the transition state

305
Q

do enzymes higher or lower substrate entropy

A

lowers it, holds it steady, makes it more ordered so it can react

306
Q

what is substrate desolvation

A

when enzymes remove H2O from around the substrate to make available all functional groups of the moelcule

307
Q

how do enzymes help specifically with induced fit

A

enzyme active sites are complementary to transtion states

308
Q

what shape does the enzyme take

A

shape that the transition state needs to be

309
Q

which step is an energy diagram is the rate limiting step

A

biggest one

310
Q

how much does an enzyme bend at the transition state

A

bends an ideal amount where it cant bend anymore so it snaps

311
Q

what can transition state analogs be

A

inhibitors

312
Q

how does the inhibitor work for the transition state

A

looks similar to the transition state but will stop it from occurring

313
Q

what is entropy based rate enhancement

A

when substrate binds to enzyme they can induce the effects illustrated by this data, by reducing entropy a reaction can happen faster

314
Q

what is rate of the rxn a function of

A

substrate concentration

315
Q

with more substrate present what does that mean for product

A

more product that can be formed

316
Q

when does the grpah of product vs time begin to flatten

A

when we run out of substrate

317
Q

what is the shape of a product vs time graph

A

rectangular hyperbola

318
Q

what is Km

A

concentration of substrate at 1/2 max rate of reaction

319
Q

Km«[S]

A

Vo=Vmax

320
Q

Km»[S]

A

Vo=Vmax[S]/Km

321
Q

what type of line is formed by Vo=Vmax[S]/Km

A

linear

322
Q

type of line formed by Vo=Vmax

A

rectangular hyperbola

323
Q

slope of a LB plot

A

slope=Km/Vmax

324
Q

y intercept of a LB plot

A

y intercept = 1/vmax

325
Q

X intercept of LB plot

A

x intercept = -1/Km

326
Q

what is the best data for a perfect enzyme

A

10^9

327
Q

why can’t an enzyme go faster than 10^9

A

bc of diffusion, 10^9 is the diffusion control limit

328
Q

units of Kcat

A

s^-1

329
Q

units of Km

A

molar

330
Q

units of Kcat/Km

A

M^-1s^-1

331
Q

what does not change in competitive inhibition

A

Vmax

332
Q

what is competitive inhibition

A

Inhibitor takes up the S spot, get enzyme inhibitor complex

333
Q

graph of competitive inhibitoion

A

lines over lap

334
Q

do good inhibitors have big or small Kis

A

small

335
Q

what shows the influence of an inhibitor in competitive inhibition

A

a

336
Q

equation for compeitive inhibition

A

1/vo=(aKm/Vmax)1/[S]+1/Vmax

337
Q

on the groah which line has no inhibitor

A

the lowest one

338
Q

examples of competitive inhibitors

A

methanol poisoning, administer ethanol to allow time for the mathanol to be secreted by the kidneys so the alcohol dehydorgenase cannot act on it and turn it to formaldehyde

339
Q

what changes with uncompetitive inhibition

A

both Vmax and Km

340
Q

what happens during uncompetitive inhibition

A

inhibitor binds to enzyme substrate complex

341
Q

what kind of graph do you get with uncompetitive inhibition

A

parallel slopes

342
Q

what shows the influence of inhibitor in uncompetitive inhibition

A

a’

343
Q

equation for uncompetitive inhibition

A

1/Vo=(Km/Vmax)1/[S] + a’/Vmax

344
Q

what are the apparent values

A

what they appear to be when the inhibitor is present

345
Q

what changes in mixed inhibition

A

both Km and Vmax

346
Q

what happens in mixed inhibition

A

inhibitor can by to Enzyme or the Enzyme substrate complex

347
Q

equation for mixed inhibition

A

1/Vo=(aKm/Vmax)1/[S] + a’/Vmax

348
Q

are amino acid residues proton donors or acceptors

A

both

349
Q

where do curly arrows start

A

at source of electrons making the new bond

350
Q

enzyme classification 1.2.3.4

A

1 is the category
2 is what is does
3 is what it does it do
4 the number classified

351
Q

what level of protein structure is HIV 1 protease

A

quaternary

352
Q

is HIV 1 protease a hetero or homo dimer

A

homodimer

353
Q

what are the substrates for HIV 1 protease

A

H2O and protein

354
Q

what is the mechanism for HIV1 protease

A

general base catlaysis of water which attacks the carbonyl carbon and generates a tetrahedral intermediate that is stabilized by hydrogen bonding

the tetrahedral intermediate then collapses; the amino acid leaving group is protonated as it is expelled

355
Q

what does the enzyme facilitae in HIV 1 protease

A

facilitate the direct attack of water on the peptide bond

356
Q

what do the HIV 1 protease inhibitors do

A

inhibit the protease and then stops the virus

357
Q

what is avoided when making drugs and why

A

chiral centers because it is too expensive

358
Q

what does enolase do

A

general acid base catalysis and metal ion catalysis

359
Q

mechanism for enolase

A

Lys345 abstracts a proton by general base catalysis,
2 of the Mg+ ions stabilize the resulting enolate intermediate
then glu211 faciliates elimination of the OH group by general acid catalysis

360
Q

what does hexokinase do

A

induced fit, with the substrate present the enzyme will close up so no water can get out, but the enzyme will only close properly with correct substrate, glucose allows it to close but xylose wont

361
Q

what is the first step in glycolysis

A

taking molecule of glucose and splitting it into 2 pyruvate

362
Q

what happens with chymotripsin

A

4 amino acids are cut out, disulfide linkages hold the chains together, these are strong so they hold onto tertiary strucutre well, in primary strcuture 122 amino acids are apart but will fold

363
Q

what do we need to do to study an enzyme

A

slow it down

364
Q

what is the optimum pH of chymotrypsin

A

8

365
Q

what are the speeds of the 2 steps of chymotripsin

A

first step is fast
second step is slow (this is where we have hydrolysis of acetic acid which was covalently linked)

366
Q

first step of chymotripsin

A

enzyme releases paranitrophenol, but it gets stuck to the product

367
Q

second step of chymotripsin

A

gets rid of the bound enzyme

368
Q

what does kcat measure

A

speeds measured at turnovers ber second

369
Q

how is chymotripsin activated

A

by proteolytic cleavage

370
Q

what is proteolytic cleavage

A

must be cut to be activated

371
Q

what does the biosynthesis of peptidoglycan require

A

enzyme transpeptidase

372
Q

what is transpeptidase inhibited by

A

B-lactam antibiotics

373
Q

what is b lactam

A

ring with 90 degree angles

374
Q

what does transpeptidase usually do

A

usually attacks the carbonyl of a peptide bonds

375
Q

what is peptidoglycan

A

mostly carbs held together by cross linking

376
Q

gram positive vs gram neg bacteria

A

gram psoitive has thick cellular walls

377
Q

how does peptioglycan contue to synthesize

A

by using trans peptidase for crosslinking

378
Q

what does the Blactam do

A

it will stop the transpeptidase and gram positive bacteria

379
Q

what has bacteria evolved to do that has caused problems

A

evolved to express B lactamases wjhoch are enzymes that can inactivate amoxilcillans and penicillans

380
Q

what is a plasmid

A

order or 1000s base of DNA

381
Q

what will the Blactamase do

A

attack B lactam

382
Q

how can enzymes be regulated

A

allosteric enzymes
reversible covalent modifications
association with regulatory proteins
proteolytic cleavage

383
Q

allosteric enzymes

A

additional binding sites when molecule binds it helps regulate

384
Q

allosteric modulation

A

activity will diverge from michaleis menten behavior

385
Q

less active enzyme

A

negative

386
Q

more active enzyme

A

positive

387
Q

what happens when something is bound to the allosteric site

A

can increase or decrease function

388
Q

example of a covalent modification of an enzyme

A

phosphorylation

389
Q

phosphoylation

A

regulation by presence based on Phosphate groups (can be truned on or off)

390
Q

what enzyme sadd phosphates

A

kinases

391
Q

what enzymes remove phosphates

A

phosphatases

392
Q

what are the amino acid residues that can gain a phospahte

A

ones with OH groups
serine
threonine
tyrosine
histidine ** N can be phosphoylated

393
Q

what is the coagulation cascade

A

blood clotting that includes several types of regulation to initiate and limit clotting

394
Q

steps of the clotting process

A
  1. activate platelets
  2. acitivate fibrin monomer formation and polymerize
  3. scab forms when polymerized fibrin cross links
395
Q

what do activated platelets do

A

changes shape, they get more negatively charged phospholipids on surface and are triggered by an injury

396
Q

what must fibrin undergo to work

A

proteolytic cleavage

397
Q

injury

A

TF released by tissue to start the clotting process, activates several proteases, fibrin will catch platelets by crosslinking

398
Q

why is Ca2+ used in the coagulation cascade

A

many steos used it, phospholipids are neagtive and are attracted to the calcium ions which helps them to interct with other proteins in the clotting process and will act as a bridge

399
Q

what shuts down the coagulation pathway

A

prothrombin which is cleaved to thrombin, thrombin will activate C and S which stops the other activation factors

400
Q

general formula for a carb

A

C(H2O)n

401
Q

When is a carb in D form

A

furthest chiral carbon with hydroxy on the right

402
Q

what is a carb

A

polyhydroxyl aldehyde or ketone

403
Q

how to find the number of enantiomers of a carb

A

2^n
n=number of chiral centers

404
Q

aldo sugar

A

carb with carbonyl on the end

405
Q

keto sugar

A

carb with carbonyl on C2

406
Q

what is more stable DNA or RNA and why

A

DNA is with one less O

407
Q

what is the relationship between an aldohexose and a ketohexose

A

isomers

408
Q

what does chirality look like in monosaccarhides

A

all monosaccharides except for dihydroxyacetone contain 1 or more chiral carbon atoms

409
Q

what is the difference in naming for pentoses

A

Ribose refers to aldo sugars and ribulose refers to keto sugars

410
Q

order of hydroxyl groups in glucose

A

RLRR

411
Q

what is an epimer

A

structure differs in the configuration at one chiral center

412
Q

beta vs alpha on a cyclic monosaccharide

A

beta is OH up
alpha is OH down

413
Q

anomeric carbon

A

carbon attached to 2 oxygens in the ring, used to be the carbonyl carbon

414
Q

a way that hemoglobin can be separated from glycated hemoglobin

A

electrophoresis

415
Q

normal glucose in blood in mM

A

5mM

416
Q

normal glucose in blood based on hospital units

A

90 mg/dL

417
Q

how do you get glycated hemoglibin

A

when hemo reacts with glucose

418
Q

what does it mean if there i 5mM of glycated hemoglobin

A

5% of the hemoglobin is gycated

419
Q

how much glcated hemoglobin is there in uncontrolled diabetes

A

7-10%

420
Q

pre diabetic range

A

100-120

421
Q

diabetic range

A

<120

422
Q

what happens with more oxidized glucose in the blood

A

the O2 must be reduced to hydrogen peroxide so enzyme test strips take the hydirgen peroxide and interact with some colorless compoind will interacts with peroxidase, the colorless compound will turn a colored product

423
Q

disaccharide

A

2 monosaccharides joined by an O glycosidic bonds (elimination of H2O)

424
Q

for dissacahrides what do you loose when you connect them

A

loose an Oxygen from anomeric C

425
Q

where is lactose found

A

in milk

426
Q

what makes up lactose

A

glucose and galactose

427
Q

is lactose a reducing sugar

A

yes bc it has a free anomeric Carbon

428
Q

where is sucrose found

A

in table sugar

429
Q

what is sucorse formed by

A

plants

430
Q

what makes up sucrose

A

glucose and fructose

431
Q

is sucrose a reducing sugar

A

no bc anomeric carbon is locked in the glycosidic linkagw

432
Q

where is trehalose found

A

in the hemolymph of insects

433
Q

what makes up trehalose

A

2 molecules of glucose

434
Q

is trehalose a reducing sugar

A

no the 2 moelcuels of glucose link the C1 together

435
Q

what makes something a reducing sugar

A

is the anomeric carbon is all tied up then it cannot be a reducing sugar

436
Q

what can a happen t reducing sugars

A

can be oxidized and then can act as a reducing agent to something else
must be able to be oxidized with a free anomeric C

437
Q

why does the reducing sugar need a free anomeric carbon

A

so that the carbon can go from aldehyde to carboxyilic acid

438
Q

why does sweetness occur

A

sweet taste is detected by receptors in the T1R2 and T1R3 in the plamsa membrane of gustatory cells in the taste buds on the tongue, bind to proteins receptor in tase bud on tongue and excite the protein coupled receptor

439
Q

what is special about aspartame as a artificial sweetner

A

looks like a protein, is a dipeptide, no c terminus but has a methyl group to make a methyl ester

440
Q

what artificial sweetner has the same chemcial formula as glucose

A

sorbital

441
Q

what is different about sorbital

A

no aldehyde or ketone so it cant become a ring, it stays linear so our body can’t break down the whole thing, can lead to diahrrea, cant be absorbed too many solutes present so water stays in the intestine

442
Q

what do the proteins and lipids on the surface of red blood cells do

A

present for a specific groupn

443
Q

what is the universal recipient

A

AB, can recieve any blood

444
Q

what can type B receive

A

B or O

445
Q

what can type A receive

A

A or O

446
Q

universal donor

A

O

447
Q

whawhat is the possibility for making more type O blood from other types

A

removing the final monosaccahride unit, tru and find enzyme that break the glycosidic linkage to turn type A into type O

448
Q

what are most carbs in nature

A

polysaccharides

449
Q

what must you identify in a polysaccahride

A

if the monosaccahirdes are homo or hetero polysaccahrises
the length of chain
bonds linking the units
degree of branching

450
Q

what are polysacchairdes used for

A

storage for fuel and structural elements

451
Q

what linkages are locked in starch

A

alpha

452
Q

what is starch a polysaccarhide of

A

glucose

453
Q

what is starch made up of

A

amylose and amylopectin

454
Q

branching of amylise

A

unbranches a1-4 linkages

455
Q

branching of amylopectin

A

branched a1-6 every 24-30 residues

456
Q

branching in glycogen

A

8-12 residues

457
Q

what are dextrans made in

A

bacteria and yeast

458
Q

what is the branching is dextrans

A

branched homo polysaccahride of glucose
a1-6 linkages, also a1-2 and a1-4

459
Q

what is peptidoglycan made from

A

repeating polysaccahirde of N acetyl glucosamine and n acetyl muramic acid, hetopolysaccahirde

460
Q

what does the peptido mean is peptidolgycan

A

cross linked by D amino acids

461
Q

what does a lysosyme do

A

breaks glycosidic bonds by hydrolysis

462
Q

where is starch made

A

in plants

463
Q

where is glycogen made

A

in animals

464
Q

what is starch and glycogen

A

storage polysaccahride in either plants or animals

465
Q

bonding in starch

A

does not hydrogen bond well, it would form a helix if it did this

466
Q

what makes up glycogen

A

all glucose

467
Q

branching in glycogen

A

a 1-4 linkages
a1-6 branches, branches every 8-12 residues

468
Q

does glycogen or strach attract water

A

glycogen

469
Q

what is the plant structural polysaccharide

A

cellulose

470
Q

where is cellulose found

A

cell walls of plants, woods, cooton

471
Q

what kind of strucutre does cellulose form

A

linear

472
Q

what will break B1-4 glycosidic linkages in cellulose

A

wood fungi

473
Q

bonding in cellulose

A

forms hydrogen bonds on itself

474
Q

what makes up cellulose

A

glucose

475
Q

where is chitin found

A

exoskeleton of insects

476
Q

what makes up chitin

A

linear N-acetylglucosamine

477
Q

linkages in chitin

A

all B becuase the molecule sometimes flips so lots of B linkages will from a linear strong dry strucutre

478
Q

does a or B hold on to water and why

A

alpha bc it is looser

479
Q

what is agar

A

mixture of sulfated heteropolysaccahrides, extracted from marine algea and seaweed

480
Q

what is agarose

A

the component of agar with the fewest charged groups (sulfates and pyruvates)

481
Q

what is the repeating unit in agar

A

galactose and a fused 6 member to 5 member ring, heteroolysaccahride

482
Q

what are glycosaminoglycans

A

carbs with amino groups

483
Q

are glysoaminoglycans intracellular or extracellular

A

extracellular

484
Q

are glycosaminoglycans hetero or homopolysaccahirdes

A

hetero

485
Q

are glycosaminoglycans positive or negative

A

negative forces extedned conformations

486
Q

what do glycosaminoglycans provide

A

viscosity, adhesiveness, and tensile strength to extracellular matrix

487
Q

examples of glycosaminoglycans

A

hyaluron, chondroiton sulfate, keratan sulfate, purified heparin

488
Q

hylauron

A

vitreous humor of the eye

489
Q

chondroiton sulfate

A

catilage, tendons and ligaments

490
Q

keratan sulfates

A

cornea, cartilage, bone and horny structures

491
Q

purified heparin

A

prevents blood clotting

492
Q

defects of glycosaminoglycans

A

synthesis or degradation

493
Q

example of a synthesis defect of glycsoaminoglycans

A

bone spur growth caused by the inability to add GlcNAc-GlcA to heparin sulfate chain
the cabs arent added correctly then bone develops extra bone growth

494
Q

what are role dextrans

A

strucutral in bacteria and extracellualr adhesive

495
Q

role of agarose

A

structural in algea

496
Q

role of hylauron

A

structural

497
Q

what are glycoconjugates

A

carbohydrates as information carriers including cell-cel communication and transportation

498
Q

what makes up a glycoprotein

A

little bit of carb lots of protein

499
Q

what does it mean to be o linked

A

attach to oxyegn on serine or threonine

500
Q

what does it mean to be N linked

A

only to N in an Asn residue must happe where N{P}-[S/T]

501
Q

what is a lipopolysaccahirde

A

Lipid A is found in the outer membrane of gram negative bacteria

502
Q

what do influenza treatments binds to

A

sialic acid binding site o neuraminidase (NA)

503
Q

how to analyze carbs

A

must first detatch the carb from the protein an enzyme will help to break that linkage, once separaed the info has to be pieced back together

504
Q

mass spec analysis of complex carbs

A

get fractionation and piece the monosaccharide together

505
Q

gene

A

segment of a DNA molecule that contains information required for the synthesis of a functional biological product i.e. protein or RNA
all the DNA that codes for a single functional polypeptide chain

506
Q

chromosome

A

single large DNA moelcule and its associated proteins (and often regulatory and structural RNA) containing many genes

507
Q

normal number of chromosomes in humans

A

46

508
Q

nucleotide

A

all 3 parts: base, ribose and phosphate

509
Q

nucleoside

A

base and ribose

510
Q

where is the base attached to in a nucleotide

A

c1

511
Q

where is the phosphate attached to in a nucleotide

A

c5

512
Q

purine shape

A

2 rings

513
Q

pyrimidine shape

A

1 ring

514
Q

what are the purines

A

adenine guanine

515
Q

what are the pyrimidines

A

cytosine
uracil
thymine

516
Q

what is the least polar part of the nucleotide

A

base

517
Q

characteristics of all bases

A

aromatic
planar
neutral (no charge)

518
Q

sp2 geometry

A

tirgonal planar

519
Q

sp3 geometry

A

tetrahedral

520
Q

what conditions is RNA hydrolyzed in

A

alkaline

521
Q

what is alkaline conditons

A

basic

522
Q

UV absorbance of DNA

A

260 nm

523
Q

base composition between species

A

varies

524
Q

compoisiton between different tissues of same species

A

same composition

525
Q

base composition does not change with

A

age, nutrition, or changing environment

526
Q

what does DNA form

A

stable double helix

527
Q

what is the largest width of DNA

A

20A

528
Q

how long is a complete turn of DNA

A

36 A

529
Q

what cnonects the bases in DNA

A

phosphodiester bonds link C3 to C5 of the ribose ring

530
Q

which bases pair together and how many bonds

A

A-T/U (2)
G-C (3)

531
Q

replication of DNA

A

each parents strand acts as a template for the biosynthesis for complementary daughter strands

532
Q

endo

A

means C2 or C3 on the ribose is up

533
Q

exo

A

means C2 or C3 on ribose is down

534
Q

the DNA backbone is stiff or flexible

A

flexible

535
Q

common forms of DNA

A

A
B
Z

536
Q

A form of DNA

A

dehydrated DNA (often in crystal structures)

537
Q

B form of DNA

A

most common/stable for random sequence

538
Q

Z form of DNA

A

occurs with alternating pyrimidines and purines ie (CG)n sequnece

539
Q

weight difference between A, B, Z form

A

all weigh the same

540
Q

what hand is the B form

A

right handed

541
Q

diameter of the B form

A

20A

542
Q

base pairs per helical turn of the B form

A

10

543
Q

helix rise per base pairs in B form

A

3.4A

544
Q

base tilt normal to the helix axis

A

6 degrees

545
Q

sugar pucker conformation of the B form

A

C-2 endo

546
Q

glycosyl bond conformation of the B form

A

anti

547
Q

what does palindrome mean

A

DNA sequence is complementary to itself

548
Q

what is a way that DNA denatures

A

heated beyond melting temp

549
Q

term for DNA strands separating

A

denaturing

550
Q

term for DNA strands going back together

A

annealing

551
Q

when DNA denatures is there an increase or decrease in viscosity

A

decrease

552
Q

ways to disrupt hydrogen bonds

A

heat
pH extremes

553
Q

what does metling temp of DNA depend on

A

pH and ionic strength of the solution in addition to GC content

554
Q

how can DNA denaturation be monitored

A

viscosity measurements or UV measurements

555
Q

hyperchrombic effect

A

increase in UV absorbption

556
Q

deamination

A

NH2 to a =O

557
Q

depurination

A

lose a base

558
Q

what is more common deamination or depurination

A

deamination

559
Q

what are ways that DNA can be damaged

A

Deaminating agents
alkylating agents
oxidative damage

560
Q

deaminating agents

A

nitrates and nititres are often used as perservatives and can result in nitrous acid which accelerates deamination reactions

561
Q

alkylating agents

A

add carbon containing group to be added to bases preventing base pairing

562
Q

oxidative damage

A

H2O2, OH radicals, O2- cause oxidation of deoxyribose strand breaks and oxidation of bases

563
Q

what can form prymidine dimers

A

UV damage

564
Q

what is more stable ds DNA or dsRNA

A

dsRNA

565
Q

mRNA

A

transfers genetic info from DNA to ribosome, forms a single stranded helix with base stacking

566
Q

tRNA

A

single stranded with significant hyodgren bonds, some regions with helix, ltos of non standard hydorgen bonds

567
Q

rRNA

A

in ribisomes, site of protein synthesis

568
Q

enzyme cofactors in nuceltides

A

helps enzyme function

569
Q

what does adenosine do in the nuecleotide

A

does not participate directly in the primaru function but is required for the cofactor or substrate to bind to the enzyme

570
Q

what else can enzyme co factors be

A

energy cofactors:ATP

571
Q

why are the nucleitide co factos so large

A

only involve the one potion, but the large cofactor allows for more affintity it can have for the enzyme,

572
Q

why do the products in ATP breakdown have lower energy then the substrates

A

more products then substrates entropy goes from 2–>3 so more disorder (lower entrioy = more disorder)
substrates are highly strained -4 on ATP and is releiced on the ADP
more resonance structures on HPO42- (more stable)

573
Q

special about DNA synthesis

A

chemical synthesis

574
Q

is DNA synthesis automated or manual

A

automated

575
Q

what end of the strand is DNA syntheized from

A

3’

576
Q

primer

A

short sequence of DNA, chemcially syntheiszed, happens very quick and cheap with increased accuracy

577
Q

what is needed for DNA syntheiss

A

protecting groups

578
Q

what is PCR

A

polymerase chain reaction

579
Q

what is needed for PCR

A

template DNA
primers (forward and reverse)
dNTPs (building bocks)
Thermostable DNA polymerase
thermocycler

580
Q

polymerase

A

enzyme that reads template and makes copies

581
Q

what does the thermostable DNA polymrase do

A

synthesizes the 2 new strands, work at 72 degrees C

582
Q

why is it important for the polymerase to work at high temps

A

it wont unfold at high temps

583
Q

what does the thermocyler do

A

instrument that carefully controls temp

584
Q

how does DNA polyemrase know when to stop

A

it doesnt, 1st, 2nd, 3rd long peices but later rounds will be correct size bc it cant go any furhtr

585
Q

what is needed for DNA sequencing by the sanger methods

A

template DNA to be sequenced
primer DNA sequence
dNTPs
ddNTPs
DNA polymerase

586
Q

why is ddNTP needed for sanger DNA sequencing

A

cayses DNA syntheis to stop bc there is no O to continue

587
Q

limitations to sanger sequencing

A

too slow and requires primers

588
Q

imporvements of 1st gen sanger sequencing

A

can be done in 1 tube, separate sizes with specific analysis. each base has a different lable

589
Q

what can the new novaseq do

A

seqience 45 whole genomes at once
average a human gemome per hour
current cost is 1000$ oer genome

590
Q

what does illumina sewuencing make use of

A

flurescent lables, much more sensitive than absorbance measures

591
Q

what is not needed in illumina sequencing

A

primers

592
Q

limitations of SMRT sequencing

A

polymerase gets electrocuted or falls off
loading long pieces of DNA

593
Q

SMRT sequencing steps

A

long sewuence of DNA flow cell–> immobilize DNA pol in the flow site –> in a circle so it can be read multiple times –. flourescent lable on the phopshate

594
Q

what is the central dogma

A

DNA is transcribed into RNA which is translated to a protein

595
Q

what must happen for DNA cloning

A

separating a specific gene or DNA segment from a larger chromosome

596
Q

what do we do with the separated gene in DNA cloning

A

attach it to a smaller molecule of DNA like a plasmid or vector

597
Q

what do we do to get the DNA to replicate

A

replicate it millons of times by introducing it into a fast multiplying host

598
Q

what must happen for the DNA to be taken up by the plasmid

A

weaken the hydrophobic effect with heat

599
Q

what is the first step of cloning

A

use restriction enzymes to cleave cloning vector (plasmid)

600
Q

what is the second step of cloning

A

obtain specific gene to interest “insert” from chromosome of organism of interest via PCR and cleave with same restriction enzyme

601
Q

what is the third step of cloning

A

ligate the DNA fragments

602
Q

what is the 4th step of cloning

A

transform bacterial host cell

603
Q

what is the 5th step of cloning

A

selectively multipy host cell in antibiotic containing media

604
Q

what do plasmids contain

A

multiple cloning sites

605
Q

why is it good that plasmids have lots of cloning sites

A

allows you to use different enzymes (enzymes used with buffers that work with both in optimal conditions)
put sticky ends on genes of interest (cut ends wihtou cutting out gene of interest (need options for where to cut)

606
Q

what types genes do some plasmids contain

A

antibiotic resistent genes

607
Q

genome

A

all the genetic information contained by an organism: genes + regulatory sequneces + non coding DNA

608
Q

how much of the human genome is composed of exons

A

1.5%

609
Q

exons

A

coding DNA

610
Q

how much of the human genome is introns

A

28.5%

611
Q

what percent of our human genome is not genes

A

70%

612
Q

what becomes part of the final mRNA

A

exons

613
Q

how many base pairs make up a nucleosome

A

146

614
Q

how many proteins make up the nucleosome

A

8

615
Q

how many proteins make up the nucleosome

A

8

616
Q

what are histone proteins modified by

A

methylation, acetylation/deactylation, and phosphorylation

617
Q

what part of the histone does the DNA actualy wrap around

A

H1

618
Q

other parts of the HIstone

A

2 of H2A, H2B, H3, H4

619
Q

dsDNA–> RNA

A

transciption

620
Q

what type of RNA is transcribed

A

messenger RNA

621
Q

what is used to synthesize the RNA comp strand to template strand of duplex DNA

A

DNA dependent RNA polymerase uses ribonuceoside 5’ triphosphate

622
Q

where does the RNA polymerase bind

A

to the promoter sequence at the 5’ end of the gene to be transcribed

623
Q

where does transcription end

A

termination sequence

624
Q

orientation of the template strand

A

3’-5’

625
Q

mRNA synthesized in what orientation

A

5’-3’

626
Q

what do the Mg ions do in transcirption

A

co factors, DNA is neg so Mg will gelp hold it in the active site

627
Q

mRNA –> protein

A

translation

628
Q

what direction is mRNA read

A

5’ to 3’, one codon at a time protein syntheiszed N to C term

629
Q

is tranaltion fast or slow

A

fast and accurate

630
Q

what is mRNA read by

A

adapter tRNA molecules

631
Q

where does translation occur

A

ribosome

632
Q

what percent of the ribosome is rRNA

A

65%

633
Q

what percent of the ribosome is protein

A

35%

634
Q

what is challenge for getting the crytal structure of rRNA

A

need crystal strucutre of all the prtoeins involed , must separate and collect fragments by centrifugation

635
Q

the genetic code is

A

nearly universal

636
Q

how many different tRNAs are there

A

32

637
Q

what is the sequence of bases on the end of a tRNA adapter molecule

A

anticodon

638
Q

what direction is the anticodon read

A

3’-5’

639
Q

at what end of the trNA is the amino acid

A

3’

640
Q

why is it good that we only have 32 tRNAs

A

speed (dont need to test as many tRNAs)
weaker bonds allow for quicker dissociation

641
Q

how are amino acids activated

A

the tRNA is aminoacylated

642
Q

initiation for tranlation

A

the mRNA and aminoacylated tRNA bind to the small ribosomal subunit, the large subunit then binds

643
Q

elongation for translation

A

succesive cycles of aminoacylated tRNA binding and peptide bond formation occur until the ribosome reaches a stop codon

644
Q

termination in translation

A

translation stops when a stop codon is encountered. the mrna and protein dissociate and the ribosomal subunits are recycled

645
Q

last part of tranlation

A

protein folding and postranslation processcing

646
Q

what happens in post translational processing

A

sugars added, 1st tRNA amino acid is cut

647
Q

start codon

A

AUG

648
Q

what is a polysome

A

multiple ribosomes can be attached to the RNA

649
Q

what do most lipids contain

A

faty acids

650
Q

whatt is a fatty acid

A

carboxylic acid, long hydrocarbon chain (nonpolar), even number of carbons (usually), somes unsaturated (non conjugated, cis double bonds)

651
Q

what is an explicit double bond

A

Sp3 carbon inbetween Sp2 C , not conjugated

652
Q

what does melting point and solubility of fatty acids depend on

A

depends on chain length and degree of saturation

653
Q

what type of interactions cause fatty acids to associate

A

weak
non covalent

654
Q

saturated fatty acid

A

very solid, no double bonds, well packed

655
Q

unsaturated fatty acid

A

has double bonds, more liquid bc of the kink formed by the double bond

656
Q

what is the melting point of a fatty acid with more double bonds

A

higher melting point

657
Q

what is the melting point of a longer fatty acid

A

longer they are the higher the melting point

658
Q

triacylglycerol or triglyceride

A

glycerol and 3 fatty acids linked by ester bonds

659
Q

where are triglycerides stored

A

in fat cells called adipocytes

660
Q

how much energy can be stored in lipids

A

weeks to months of energy sotred

661
Q

what do biological membranes consist of

A

lipid bilayer

662
Q

characterisic of membrane lipids

A

amphipathic (polar and non polar ends)

663
Q

what are the. 5types of membrane lipids

A

glycerophospholipids
galactolipids and sulfolipids
archeal tetraether lipids
sphingolipids
sterols

664
Q

what holds lipids together in the bilayer

A

hydrophobic effect (non polar tails away from water)

665
Q

what keeps a singular lipid together

A

covalent bonds

666
Q

lot or little entropy in the lipid bilayer

A

lots (all are constantly moving around, have lots of freedom)

667
Q

what is a phospholipid composed of

A

phosphate
glycerol
fatty acid tail

668
Q

glycerophospholipid or phosphoglycerides

A

2 fatty acids + glycerol + phosphate + head group

669
Q

what part of the lipid determines the net charge on moelcuels

A

head group

670
Q

galactoplipids and sulfolipids

A

polar head group is galactose or glucose with or without a sulfate group. common in plants where soil phosphate supply may be limited

671
Q

archeal lipids

A

8 isoprene units per chain
ether linkage is very stable
thirve in extreme conditions

672
Q

what is special about archeal lipids

A

monolayer all nonpolar parts in middle, both ends are polar

673
Q

why wont archeal lipids melt apart

A

lots of branch points built fro 5C isoprene unit

Biochem (4 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions