Brainscape's Knowledge GenomeTM

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


See full index

Cell Biology > Ch 3/ Protein Structure and Function > Flashcards

Ch 3/ Protein Structure and Function Flashcards

1
Q

Non polar ameno acids letters

A

(London & Canada (C for cys)

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

Uncharged polar ameno acid letters

A

NQSTY

Quit The Nozzey Shit You

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

Basic ameno acid letters

A

(positve)

RKH

Kyle Rests Heavaly

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

acidic ameno acid letters

A

Negative

DE

Dead Earth

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

unique properties of water

A

given by H bonds

are thermal regulation and universal solvent

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

Disolves in water

A

ionic and polar

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

hydration shells

A

keeps ions seperage (also polar molecules), partal charge on O of water is attracted to ions making the schell

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

hydrophobic effect

A

nonpolar subsances excluded from solvation netwoek of water

hydrophobic results in few water milecules on scheel, therefore released and spontatious

nonpolar has an orderd water chage, unfavered

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

high number of hydrocarbons

A

non polar

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

protines add

A

functionality

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

functions of protines

A

structural, movement, defence, regulation, transport, catalusis

SM(all)

D(i)R(t)

T(i)K

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

each protine folds into a

A

stable conformatin

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

parts of ameno acid

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

Unchared polar

A

capable of forming H bonds

H & OH-

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

Nature prefers on __ over another

A

issomer

L ameno acids

D suggars

same with enzimes

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

chiral

A

4 differnt groups

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

Thalimonide

A

was racemic mixtre one form sedative other caused brith defects

not even just give one enantomer - because boddy convers it tothe other

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

___ site on enzimes (are chiral)

A

allosteric site

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

Peptide bond

A

covalent bond

connects two amino acids

amide linkage

e- is delocalized - exists as resonance

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

formation of peptide bond

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

type of reaction of peptide bond

A

condensation, dehydration,

Nuc. Acytl sub.

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

How peptide bond affects protine conformation

A

rigid and planer

partial double bond charatar (b/c resonance)

not rotate freely (1/3 of bonds in peptide backbone)

limits conformation possibilites of protines

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

Primary

A

linear ameno acid sequence

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

secondary

A

basic folding units (helices, sheets)

Common patterns

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

tertiary

A

3D structre of a folded prien (final)

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

Quaternary

A

contains more than one polypeptide chain

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

Priamary structure is listed from __ to __

A

N (amino) terminous to C (carboxyl) terminous

28
Q

the backbone of the polpeptide excludes __

is a repeating __

A

r chains

repeating CCN

29
Q

3D structure is determined by the

A

order of amino acids

30
Q

alfa heliex Bondong:

R group:

philic:

A

hydrogen bonding between N-H and c=O groups in polypeptide backbone (every 4 amino acids)

Rgroup away from helix

one side is hydropobic other side is hydrifilic (amphipathic)

31
Q

coiled coil

A

supper seoncdary

alpha helies wrap around each other to form a stable sturctre

two amphipathic come together (phobic binds w phobic phillic binds with phillic)

32
Q

Betta sheet

A

when polpeptide chain segments line up side by side

each Betta sheet is fully extended and stabalized by H bonding between N-h and carboxl groups WITHIN the polypeptide backbone

also amphipathic - goes above and below the plane, the R groups alternate up and down

33
Q

spider silk

A

stronger than steel

34
Q

pick sequenct that could fom a strand in a amphipathic beta sheet

A

alternating polar and nonpolar ameno acids

35
Q

tertiart structre

A

interacts of side chains/r groups

36
Q

Protine domains

A

substucture

fold independantly into a stable compact structre

each doman is a specific function of the protien (and structure)

37
Q

Globular protiens

A

soluable in H2O, compact structre, synamic function

38
Q

Fibrous protines

A

structural protines, long rod shape, insoluable in water

39
Q

Non covalent interactions include

A

vander wals

H bonding

electrostatic attractions

40
Q

vander wals

A

weak fromed with in close range between non polar atoms

fluctuate electtral charges in close proximity

41
Q

H bonding

A

between hydrogen attom and small highly electroneg attom

42
Q

electrostatic attrations

A

salt bridges

attration between ionic groups of opposite charges (ex. ionic bonds between acid and basic)

43
Q

Disulfide bridge/bond

A

forms when two cysteine residues are oxidized

SH SH to S S

44
Q

Hemoglobin quaternary structure

A

2 alfa 2 beta chains

each has a heme group that binds to oxygen (like a “pocket”)

2 dimers slide past each other

45
Q

indivdual subunits of multimeric complexts ___ associate to from a __

A

non-covalentaly (alows functionality because break and form eaisly)

a functional protine structure

46
Q

problem of protine folding

A

cannot go though all possible conformations

protines take less than a second to fold inside cell or in test tube

47
Q

Levinthal’s paradox

A

astronomcal numbers of conformations open to a protine in a denatured state

48
Q

molten globule

A

protein states that are more or less compact, but are lacking the specific tight packing of amino acid residues which creates the solid state-like tertiary structure of completely folded proteins.

formation of tertiary strutures but not fully there

49
Q

Native proteins

A

lowest energy form/ bottem of energy landscape model

50
Q

intermediates of energy landscape model

A

are more stable

51
Q

the folding code

A

themodynamic question of folding causes less disorder but it is spontanous (inc disorder in universe) how

52
Q

protine structure prediction

A

predit proteins native structre froma ameno acids

53
Q

the folding process

A

kientics

a lof of possible pathways, how does it know which to take

54
Q

glibular proteins are __ proteins

A

soluble

55
Q

hydrophobic groups together in aquesous enviorment

A

hydrophobic groups togerher, water gets released into surroundsings (from water schell), increasing disorder

56
Q

Minimizing the nonpolar surface area
(bury nonpolar groups in interior of
folded protein) minimizes the

A

number of water molecules that become
ordered

water is freed, no longer organized aeound polpeptide

57
Q

denaturing of albumin in egg goes from

A

soluable to insoluable

58
Q

denaturing conditions

A

heat

reducing agents

detergents

high salt

mechanical stress

59
Q

heat

A

disrups weak bonds such as H

60
Q

Reducing agents

A

disulfide brige (covalant bond) is produced durring oxidation and removed with reduction

61
Q

detergents

A

get more on thiss

amphipathic - hydrophobic and hydrophilic

62
Q

high salts

A

distrupt ionic bonds

63
Q

mechanical stress

A

ex. whisk egg white causes foam (with denatured protines)

64
Q

ligand

A

substance bound by the protine

65
Q

Indicate level(s) of protein structure to which
each of the following contributes:
a. hydrogen bond
b. beta pleated sheet
c. disulfide bond
d. amino acid sequence

A

a. secondary, tertiary (quantanry if accaplable)
b. secodary
c. tertairy (quant if apiciable)

d primary

66
Q

disulfide bond is caused by

A

teo cistines reducing

Cell Biology (7 decks)

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