Biochem Digging Up Bones Flashcards
(102 cards)
1
Q
DNA TO DNA
A
Replication
2
Q
DNA TO RNA
A
TRANSCRIPTION
3
Q
RNA TO PROTEINS
A
Translation
4
Q
H+ acceptor
A
Base
5
Q
H+ donor
A
Acid
6
Q
Donates few of its H+
A
Weak acid
7
Q
Donates almost almost all of its H+ and forms a weak conjugate
A
Strong acid
8
Q
A solution that resists changes in its pH when acid or base are added
A
Buffer
9
Q
The migration of water from the side of a membrane that is hypoosmotic to the side that is hyperosmotic
A
Osmosis
10
Q
Facilitated transport of a molecule down the concentration gradient by a carrier, does not use energy
A
Passive transport
11
Q
Facilitated transport of a molecule down the concentration gradient by a carrier, uses energy
A
Active transport
12
Q
Types of co-transport
A
Symport
Antiport
13
Q
Process by which matter from the outside an organism is transformed into energy or material for the organism
A
Metabolism
14
Q
Reactions that break the bonds of complex molecules
A
Catabolism
15
Q
Reactions which synthesize complex molecules from simpler molecules
A
Anabolism
16
Q
Energymedium for reqctions inside the cell
A
ATP
17
Q
Loss of electron
A
Oxidation
18
Q
Gain of electrons
A
Reduction
19
Q
Carbohydrate yields # kcal
A
4kcal/gam
20
Q
Protein yields # kcal
A
4 kcal/gram
21
Q
Alcohol yields # kcal
A
7kcal/gram
22
Q
Fats yields # kcal
A
9kcal/gram
23
Q
Excretory form of protein
A
Urea
24
Q
Bacteria cqn metabolize urea to ?
A
Ammonia
25
Where is ethanol is metabolized?
Liver
26
Alcohol inhibits ?
Gluconeogenesis
27
Starch is made in these 2 sites
Liver
| Muscle
28
It is the major energy store in the body
Fat(triacylglycerol)
29
2 Sources of monounsaturated fats
Olive oil
| Canola oil
30
All plants have unsaturated fats except 2?
Coconut oil
| Palm oil
31
Energy source utilized by muscle at rest? Active?
At rest: Fat
| Active: Carbohydrates
32
Energy source utilized by brain?
Carbohydrates
33
Number of amino acids in animal metabolism
20
34
ESSENSTIAL AMINO ACIDS
phenylalanine, valine, tryptophan, threonine, isoleucine, methionine, Histidine, Argninine, Lysine
[PVT TIM HAL] always trys never tyrs
35
An amino acid with a sidechain that forms a ring with the amino group of the back bone
Proline
36
These amino acids are hydrophobic and bond together through hydrophobic interactions
Valine, Leucine, isoleucine
37
amino acids with aromatic side chains
phenylalanine, tyrosine, tryptophan
38
amino acids that contain sulfur
cysteine, methionine
39
an imino acid and forms a ring with its own backbone
proline
40
determine the function of the protein
side chains
41
nonpolar side chains, hydrophobic or hydrophilic?
hydrophobic
42
Polar acidic amino acids
aspartate glutamate
43
polar basic amino acids
histidine arginine lysine
44
amino acid that has an imidazole ring, offers buffering at physiologic pH to protein. decarboxylated to histamine
histidine
45
2 amino acids that contain hydroxyl groups which can ofrm hydrogen bonds
serine and threonine
46
formed by a disulfide bond joining 2 cysteine residues
cystine
| keratin has many cystine
47
amino acid used in the first step of heme synthesis
Glycine
48
blood glycoproteins in diabetics contains glucose linked to this amino acid
lysine
49
amino acid with the largest side chain, it is hydrophobic with an aromatic ring
tyrosine
50
deficiency of this amino acid can cause hartnup disease and pellagra
tryptophan ( coverted to niacin)
51
amino acids that carries nitrogen from the periperal tissues to the liver
Alanine glutamine
52
amino acid disrupts the a-helix in a polypeptide
proline
53
this amino acid is the phosphorylation site of enzyme modification
serine
54
amino acid deaminated to form ammonia
glutamine
55
dipolar ions
zwitterion
56
essential amino acids
(PVT TIM HALL always trys never tyrs)
| phenylalanine valine tryptophan threonine isoleucine methionine leucine lysine
57
relatively essential amino acids
histidine arginine
58
none essential amino acids
(PACT)
| proline, arginine(adult) , cysteine, tyrosine
59
disease resulting from adequate inadequate intake of protein, but adequate intake of calories
kwashiorkor
60
disease resulting from inadequate intake of both calories and protein
marasmus
61
disease presents with unpigmented hair which appears reddish, fatty liver, edema, protruding abdomen
kwashiorkor
62
disease presents with retarded growth, emaciation, cachexia, but now low albumin or edema
marasmus
63
sequence of amino acids in a polypeptide chain
primary structure
64
hydrogen bonding which produces regularly repeated structures( alpha helix and b pleated sheets)
secondary structure
65
overall 3 dimensional shape of the protein
tertiary structure
66
a number of subunits with spatial arrangement
quarternary structure
67
Peptide bonds are formed by joining amino acids by this reaction
dehydration
68
Dehydration reaction that forms the peptide bond can be reversed by this reaction
hydrolysis
69
all peptide bonds of a polypeptide chain will be broken and the individual amino acids released in this condition
strong acid solution at 43°C(110°F) for 24 hours
70
amount of energy which must be added to a reaction to allow it to go forward
Gibb's free energy of activation
71
rate that a reaction occurs
reaction velocity
72
increases the speed of a reaction by lowering the reactions energy of activation
catalysts
73
protein catalyst which may require a vitamin or mineral cofactor
enzyme
74
catalyzes reactions adding or removing nucleoside triphosphate(usally ATP)
kinase
75
removes H+
dehydrogenase
76
the substance which is recognized by the enzyme and is transformed into the product of the reaction
substrate
77
substance formed by the interaction of the substrate and enzyme
product
78
part of the enzyme which is catalytic
active site
79
attraction between enzyme and substrate
affinity
80
theory which states substrate and enzyme always fit each other
Lock and key theory
81
theory which states substrates and enzyme fit only at binding
induced fit theory
82
enzymes which have different amino acid sequences, but catalyze the same reactions
isoenzyme
83
An enzyme which requires a cofactor to be active
holoenzyme
84
protein part of a holoenzyme
apoenzyme
85
a cofactor which is permanently complexed with its enzyme
prosthetic group
86
enzyme which contains another site, different from the active site, at which an effector binds
allosteric enyme
87
An enzyme whose substrate is also its effector
homotrophic enzyme
88
an enzyme which has a different molecule as an effector
heterotrophic enzyme
89
enzyme which may increase or inhibit substrate binding, binding to one site can alter other sites. sigmoidal plot, as opposed to michaelis menten kinetics(hyperbolic)
allosteric enzyme
90
activating or inactivating regulatory enzymes
phosphorylation
activator- phosphorylase
deactivator- phosphatase
91
Factors that affect the rate of a reaction
substrate concentration
temperature
pH
92
Kinetic order: reactions where the rate is independent from substrate concentration
zero order
93
Kinetic order: rate is independent from substrate concentration; proportional
first order
94
enzymes that have a hyperbolic curve
michaelis-menten equation
95
this equation rearranges the michaelis-menten equation so that the line plotted is straight
lineweaver-burke plot
96
inhibitor is shaped similar to the substrate and temporarily competes with it for binding sites
competitive inhibition
97
binds temporarily to enzyme somewhere other than active site but halts catalysis
non-competitive inhibition
98
bind covalently to enzymes and permanently inactivates them
irreversible inhibitors
99
catalyze irreversible reactions and are usally the committe step in the pathway
allosteric enzyme
100
change in heat of reactants and products
enthalpy
101
change in randomness or disorder of the reactants and products
entropy
102
reaction occurs spontaneously when change is negative, and not spontaneous when positive
free energy
