Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Biology 1 (Molecules) > 1. Molecules and Enzymes > Flashcards

1. Molecules and Enzymes Flashcards

(77 cards)

Start Studying
1
Q

hydrogen bonding

A

intermolecular bonding between H and F, O, or N

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

can lipids pass through cellular membranes?

A

yes

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

fatty acids

A

fuel and components of cell membranes
long chain of carbons
carboxylic acid on the end

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

saturated fatty acids

A

single carbon-carbon bonds

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

unsaturated fatty acids

A

at least one carbon-carbon double bond

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

triaglycerols

A

three-carbon backbone (glycerol) and three fatty acid chains
store energy and insulate

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

phospholipids

A

lipids with phosphate group attached
i.e. phosphoglycerides (glycerol backbone, phosphate group and fatty acid chains)

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

amphipathic

A

polar on one end, non-polar on the other

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

sphingolipids

A

polar head group and long chain fatty acid
backbone is sphingosine
part of cell membrane

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

steroids

A

four-ringed
cholesterol
membrane component (stability and fluidity)

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

waxes

A

ester linkages between long-chain alcohol and long-chain fatty acid
water-repellent

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

prostaglandins

A

eicosanoids
released from cell membrane and act as local hormone

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

is protein denser than lipid?

A

yes

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

which stores more energy? carbs or lipids

A

lipids because higher concentration of C-H bonds

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

polysaccharides

A

multiple carbohydrates

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

glycogen

A

glucose polymer

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

beta linkages (carbs)

A

cannot be broken down by animals

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

nucleotide structure

A

five carbon sugar
nitrogenous base
phosphate group

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

nucleoside vs nucleotide

A

nucleoside lacks the phosphate group

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

phosphodiester bonds

A

between phosphate of one nucleotide and third carbon of sugar on the other nucleotide

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

purines

A

adenine and guanine

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

pyrimidines

A

cytosine and thymine/uracil

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

what type of bond holds the two strands of DNA together?

A

hydrogen bonds

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

base pairing rules

A

adenine with thymine (2 H-bonds)
guanine with cytosine (3 H-bonds)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
differences in RNA
carbon 2 on the sugar is not deoxygenated (has hydroxyl) single-stranded uracil instead of thymine can move through nuclear membrane
26
peptide bond
covalent bond that joins two amino acids by removing a water molecule from one and a carboxyl group from another dehydration reaction
27
glycine
Gly G non-polar
28
alanine
Ala A non-polar
29
valine
Val V non-polar
30
leucine
Leu L non-polar
31
isoleucine
Ile I non-polar
32
phenylalanine
Phe F non-polar
33
tryptophan
Trp W non-polar
34
methionine
Met M non-polar
35
proline
Pro P non-polar
36
serine
Ser S polar
37
threonine
Thr T polar
38
cysteine
Cys C polar
39
asparagine
Asn N polar
40
tyrosine
Tyr Y polar
41
glutamine
Gln Q polar
42
aspartic acid
Asp D polar acidic
43
glutamic acid
Glu E polar acidic
44
histidine
His H polar basic
45
lysine
Lys K polar basic
46
arginine
Arg R polar basic
47
polar amino acids stabilize polar substrates with...
hydrogen bonding
48
non-polar amino acids stabilize non-polar substrates with...
Van der Waals interactions
49
if an amino acid is acidic this says what about the enzyme's active site?
it is probably negatively charged
50
primary structure
sequence of amino acids (polypeptide)
51
secondary structure
polypeptide twists into alpha-helix or beta-pleated sheets (reinforced by H-bonds)
52
tertiary structure
three-dimensional shape formed by folds of peptide chain covalent disulfide bonds ionic interactions (electrostatic) H-bonds Van der Waals hydrophobic bonding at the center
53
quaternary structure
two or more polypeptide chains bind together same forces as in tertiary structure
54
denatured protein
when native conformation is disrupted does not disrupt primary structure
55
disulfide bond
between two cystine amino acids on different parts of the chain
56
catalysts
lower activation energy of a reaction increase rate of reaction
57
lock and key model
enzyme active site has shape for specific substrate
58
induced fit model
shape of enzyme and substrate are altered upon binding
59
saturation kinetics
as the relative concentration of substrate increases, the rate of reaction also increases, but to a lesser and lesser degree until a maximum rate (Vmax)
60
Vmax
maximum rate of reaction for enzyme catalyzed reaction
61
kcat
turnover number catalytic efficiency number of substrate molecules one active site can convert to product in a given time
62
Km
Michaelis Constant substrate concentration at which reaction rate is equal to 1/2Vmax intrinsic quality
63
Km is inversely proportional to...
enzyme-substrate affinity
64
co-factor
coenzyme or metal ion
65
zymogen
inactive form of enzyme
66
allosteric interactions
modification of enzyme configuration through the binding of an activator or inhibitor at a binding site on the enzyme (not the active site)
67
positive cooperativity
the first substrate changes the shape of the enzyme allowing other substrates to bind more easilyq
68
competitive inhibitor
bind reversibly to active site raise Km no change Vmax (add more substrate)
69
uncompetitive inhibitor
bind at site other than active site once associated with substrate Km decreases (they are stuck together) Vmax lowered
69
non-competitive inhibitor
bind to E-S complex or enzyme at site other than active site no change Km lower Vmax
70
oxidoreductases
transfer of electrons or H ions
71
transferases
groups are transferred from one location to another
72
hydrolases
hydrolysis reactions
73
lyases
functional groups added to double bonds, or removed to form double bonds
74
isomerases
transfer of group within molecules
75
ligases
condensation reactions coupled with the hydrolysis of high energy molecules
76

Biology 1 (Molecules) (4 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions