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BIOCHEM Flashcards

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1
Q

aliphatic means:

A

nonaromatic

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2
Q

how many H bonds does C (cytosine) make with G (guanine)

A

3

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3
Q

how many H bonds does T (thymine) make with A (adenine)

A

2

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4
Q

adding more bonds to H

A

reduction

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5
Q

adding more bonds to oxygen

A

oxidation

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6
Q

a kinase is an example of what type of enzyme

A

transferase

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7
Q

a polymerase is an example of what type of enzyme

A

transferase

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8
Q

pepsin is an example of what type of enzyme

A

hydrolase

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9
Q

enzyme that switches arrangement of atoms within a molecule

A

isomerase

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10
Q

synthatase is an example of what type of enzyme

A

ligase

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11
Q

enzyme that requires ATP to function

A

ligase

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12
Q

cofactors/coenzymes present with enzyme

A

holoenzyme

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13
Q

cofactors/coenzymes not present with enzyme

A

apoenzyme

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14
Q

inorganic metal ions

A

cofactors

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15
Q

organic (vitamins)

A

coenzymes

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16
Q

inactive form of an enzyme

A

zymogen

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17
Q

metabolic pathways that take place in the mitochondria:

A

TCA, beta oxidation, and ETC

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18
Q

the site of synthesis of proteins and other molecules, such as lipids or hormones, that are destined for secretion by the cell

A

ER

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19
Q

sorts and adds modifications to molecules created by the ER, but it does not participate in protein synthesis

A

Golgi apparatus

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20
Q

bond that forms with polar head to fatty acid tails in phospholipids

A

phosphodiester bonds

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21
Q

difference b/t phenylalanine and tyrosine

A

phenylalanine: benzene ring in side chain
tyrosine: benzene ring plus -OH making it a phenol in side chain

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22
Q

non-functional tRNA would cause what

A

no proteins to be made

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23
Q

the presence of more than one mtDNA type in an individual

A

heteroplasmy

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24
Q

insert and remove themselves from a genome; when removed, gene function is restored

A

transposons

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25
Q

cleaves proteins

A

proteases

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26
Q

less protein in blood meaning a decrease in osmotic pressure

A

hypoalbuminemia

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27
Q

lactose is a mono or disaccharide

A

disaccharide

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28
Q

NADPH a reducer or an oxidizer

A

reducer; so less of this would mean more oxidation

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29
Q

is ATP hydrolysis coupled in glycolysis

A

absolutely

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30
Q

bonds that require stronger bonds than H bonds (disulfide)

A

irreversible bonds

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31
Q

enzyme involved in DNA replication and transcription that also helps with helicases function

A

topoisomerase

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32
Q

transcriptional regulatory sequences that function by enhancing the activity of RNA polymerase at a single promoter site

A

enhancers

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33
Q

what decreases transcription of genes

A

DNA methylation (think heterochromatin-very methylated)

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34
Q

an inducible system; inducer binds to repressor

A

lac operon

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35
Q

a repressible system; blocks transcription

A

trp operon

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36
Q

peptide bonds are also known as

A

amide linkages

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37
Q

located in nucleolus and synthesizes rRNA

A

RNA polymerase I

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38
Q

located in nucleus and synthesizes hnRNA and snRNA and is the main player in transcribing mRNA

A

RNA polymerase II

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39
Q

located in nucleus and synthesizes tRNA

A

RNA polymerase III

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40
Q

mRNA is derived from ____ via posttranscriptional modifications

A

hnRNA

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41
Q

rate limiting enzyme for glycolysis

A

PFK-1

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42
Q

3 irreversible steps in glycolysis:

A

1, 3, 10

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43
Q

3 enzymes involved in the irreversible steps of glycolysis:

A

step 1: hexokinase
step 3: PFK-1
step 10: pyruvate kinase

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44
Q

Net gain at end of glycolysis:

A

2 NADH
2 ATP
2 pyruvate

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45
Q

any step in TCA cycle that produces a NADH or FADH2 uses what kind of enzyme

A

dehydrogenase

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46
Q

rate limiting enzyme for TCA cycle:

A

isocitrate dehydrogenase

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47
Q

Net gain after TCA cycle:

A

6 NADH
2 FADH2
2 GTP

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48
Q

electron donors in ETC:

A

NADH and FADH2

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49
Q

electron acceptor in ETC:

A

oxygen

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50
Q

what complex along ETC does not pump protons to IMS

A

complex II

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51
Q

ATP synthase on ETC uses what to have a conformation shift to eventually make ATP

A

chemiosmotic coupling (flow of protons with conformational shift)

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52
Q

rate-limiting enzyme in glycogenolysis

A

glycogen phosphorylase

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53
Q

does glycogenolysis use branching or debranching enzyme

A

debranching

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54
Q

2 main things used in glycogenesis

A

glycogen synthase

branching enzyme

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55
Q

irreversible enzymes used in gluconeogenesis

A

step 1: pyruvate carboxylase
step 3: fructose 1,6-bisphosphatase
step 10: glucose-6-phosphatase

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56
Q

rate limiting enzyme in gluconeogenesis

A

fructose 1,6-bisphosphatase

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57
Q

total amount of ATP produced after TCA cycle and ETC

A

30-32

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58
Q

Acetyl-CoA- malonyl CoA- palmitic acid (16 C)

A

fatty acid synthesis

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59
Q

rate limiting enzyme of fatty acid synthesis

A

acetyl-CoA carboxylase

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60
Q

reducing agent in fatty acid synthesis

A

NADPH

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61
Q

how many NADPH used to make 16 C palmitic acid

A

14

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62
Q

what gets fatty acids into matrix

A

carnitine

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63
Q

breakdown of fatty acids to Acetyl-CoA

A

beta-oxidation (in matrix)

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64
Q

how many acetyl CoAs for a 16 carbon fat that is broken down

A

8

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65
Q

point of TCA cycle

A

produce NADH and FADH2

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66
Q

point of beta-oxidation

A

reduce Acetyl-CoA to enter into TCA cycle

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67
Q

breakdown what to put glucose back in blood

A

glycogen

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68
Q

a way to move Acetyl-CoA in the blood

A

ketogenesis (ketone bodies from beta-oxidation)

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69
Q

what happens when you synthesize triacylglycerol?

A

you can store fatty acids

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70
Q

2 reactions not in mitochondria

A

gluconeogenesis

glycolysis

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71
Q

how many ATP from 2 turns of TCA cycle

A

20

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72
Q

all amino acids have chiral alpha carbon except

A

glycine

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73
Q

2 amino acids have a chiral carbon in side chain:

A

threonine and isoleucine

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74
Q

AA with an ionizable side chain

A

histidine (imidazole ring- N atom that can be protonated)

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75
Q

Amino acids that are both ketogenic and glucogenic:

A

tryptophan, phenylalanine, tyrosine, isoleucine, threonine (FITTT)

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76
Q

ketogenic amino acids:

A

leucine and lysine

77
Q

glucogenic amino acids:

A

13 remaining amino acids that aren’t ketogenic and aren’t both

78
Q

amino acids that can be converted into ketone bodies are called

A

ketogenic

79
Q

amino acids that can be converted into glucose are called

A

glucogenic

80
Q

this gel disrupts disulfide bonds and would show 2 bands instead of 1 if molecule contains these bonds

A

reducing gel

81
Q

this gel disrupts non-disulfide interactions, so when there is a smaller band produced with half the weight, it consists of a homodimer (2 identical subunits)

A

SDS page

82
Q

phosphorylation occurs on these AA’s due to their hydroxyl group on side chain

A

serine, threonine, and tyrosine

83
Q

ending of enzymes involved in redox reactions:

A

-oxidase, -reductase, -dehydrogenase, -monooxygenase

84
Q

why must FAD/FADH2 be bound to enzymes?

A

b/c it can exist as a semiquinone and if bound to enzymes it won’t easily react with oxygen

85
Q

molecule that contains an imine (C=NH) and a carboxyl group

A

imino acid

86
Q

why can a reaction that is spontaneous under standard conditions also run in reverse

A

cell alters conc. of substrates (reactants)

87
Q

amine to amide when amine group acts as a ___ in a rxn

A

nucleophile

88
Q

amines vs. amides

A

amides have carbonyl group attached to N atom

89
Q

only AA that does not have a beta carbon

A

glycine

90
Q

polypeptides are named how?

A

N terminus to C terminus

91
Q

a type of fat that contains double bonds and is therefore considered unsaturated

A

trans fat

92
Q

which phosphates on ATP get transferred to other molecules by a kinase

A

gamma- phosphate

93
Q

why G-C causes higher melting temp. of DNA rich in GC content

A

stronger pi stacking interactions than A-T

94
Q

under anaerobic conditions, how many ATP are produced from 1 mole of glucose

A

2 ATP

95
Q

originate from centrosomes

A

microtubules

96
Q

4 fused rings indicative of…

A

steroid

97
Q

Keq for DNA unfolding

A

Keq= unfolded/native

98
Q

this muscle fiber type uses more mitochondria and is used for aerobic activity

A

slow twitch muscle fiber

99
Q

under low oxygen conditions (hypoxia), glycolysis works but oxidative phosphorylation won’t so how do you allow glycolysis to proceed?

A

NADH converted back to NAD+ through lactic acid fermentation

100
Q

if an inhibitor is able to have an effect on an enzyme for 7 days, what kind of inhibition does it have?

A

irreversible

101
Q

high Km means two things:

A

lower affinity and decreased reaction rate

102
Q

cytochrome P450 acts as what

A

monooxygenase- it oxidizes substrates

103
Q

function of a carboxylase

A

add a carboxyl (COO-) group to molecule

104
Q

ATP consumption and production during glycolysis

A

2 ATP consumed; 4 ATP produced

105
Q

least suitable for a vaccine

A

toxicity

106
Q

large subunit of prokaryote ribosome

A

50S

107
Q

intact prokaryotic ribosomes

A

70S

108
Q

large subunit of eukaryotic ribosome

A

60S

109
Q

intact eukaryotic ribosome

A

80S

110
Q

D54 residue means what

A

aspartate residue (D)

111
Q

K54 residue means what

A

lysine residue (K)

112
Q

separates molecules based on electrophoretic mobility; relying on length, conformation change, charge

A

Native PAGE

113
Q

separates proteins only on the basis of their size

A

Gel Filtration Chromatography

114
Q

weight of amino acid

A

110 Da

115
Q

cocaine (a stimulant) would have a physiological effect similar to what that would increase what metabolism

A

stress; increase glucose metabolism

116
Q

important enzyme that produces NADH in glycolysis

A

glyceraldehyde-3-phosphate dehydrogenase (makes sense b/c ending in dehydrogenase means producing either FADH2 or NADH)

117
Q

what enzymes perform substrate level phosphorylation during glycolysis

A

3-phosphoglycerate kinase and pyruvate kinase

118
Q

main purpose of TCA cycle

A

oxidize acetyl-CoA to CO2 and produce GTP and NADH and FADH2 for ETC

119
Q

rate limiting enzyme of Pentose Phosphate Pathway (PPP)

A

glucose-6-phosphate dehydrogenase

120
Q

chylomicrons, VLDL, IDL, LDL, and HDL transport what

A

lipids

121
Q

key enzyme in cholesterol biosynthesis

A

HMG-CoA reductase

122
Q

the only fatty acid that humans can synthesize

A

palmitic acid

123
Q

brain uses what metabolism normally? but if it’s in prolonged starvation, it uses what

A

glucose; and then uses ketolysis (ketone bodies)

124
Q

what is the shape of graph for normal MM kinetics with graph of Vo vs. substrate concentration [S]

A

hyperbolic

125
Q

used to describe the rate-limiting step of catalysis under SATURATING conditions of substrate

A

kcat

126
Q

what does Hill Coefficient do

A

tells us if something exhibits cooperativity or not

127
Q

Hill coefficient greater than 1 means

A

it will exhibit cooperativity

128
Q

these bind the enzyme and the enzyme-substrate complex with the same affinity; vmax decreases but Km remains unchanged

A

noncompetitive inhibitors

129
Q

AA’s that have amide group in their side chains

A

glutamine and asparagine

130
Q

deamidation reaction releases what

A

NH3

131
Q

separates proteins based on isoelectric point; needs to have a stable pH gradient established

A

isoelectric focusing

132
Q

this nucleotide contains 2 rings and 1 carbonyl

A

guanine

133
Q

this nucleotide contains 2 rings with no carbonyl

A

adenine

134
Q

this nucleotide contains 1 ring with 1 carbonyl

A

cytosine

135
Q

this nucleotide contains 1 ring with 2 carbonyls

A

thymine

136
Q

higher affinity corresponds to a higher or lower Kd (Km)

A

lower Kd (Km)

137
Q

hormone that is hydrophilic and soluble in blood

A

peptide hormone

138
Q

interactions that contribute to stabilization of protein structure

A

disulfide, hydrogen bonds, and salt bridges

139
Q

what attaches nucleotides together but is NOT used to stabilize protein structure

A

phosphodiester bonds

140
Q

inhibitor that binds to their target enzymes only when the substrate is first bound (only binds to enzyme-substrate complex); both Km and vmax decrease

A

uncompetitive inhibitor

141
Q

inhibitor that binds active site but doesnt allow reaction to proceed forward

A

irreversible inhibitor

142
Q

if someone is hypoglycemic, what needs to be produced more in order maintain homeostasis

A

consume more glucose; b/c our body usually breaks down glycogen into glucose, so with low levels of glycogen, there will be low levels of glucose

143
Q

without acetylcholine receptors, what won’t occur

A

depolarization

144
Q

what tissue produces fatty acids, glucose, and ketone bodies

A

adipose tissue

145
Q

location on chromosome where certain genes are known to be located; where alleles are for a gene

A

locus

146
Q

a type of frameshift mutation that usually produces nonfunctional protein, but if inserted towards end of gene, could potentially produce functional protein

A

insertion mutation

147
Q

methylation increases or decreases stability

A

increases

148
Q

stability of DNA and RNA is largely dependent on what

A

amount of GC pairs

149
Q

melting temperature (Tm) definition

A

point when 50% of molecules have been denatured

150
Q

in aqueous solution, what areas will tend to aggregate together so that polar areas will have maximal contact with one another/the solution

A

hydrophobic

151
Q

1 amino acid weight in Da

A

110 Da

152
Q

when dealing with melting point, what do you look at on amino acids compared to other molecules?

A

Look at both NH2 and COOH- those alone contribute to interactions that would lead to higher melting point than say a ethanol; don’t just look at side chain

153
Q

only alters rate and activation energy; not Gibbs or delta H

A

enzyme

154
Q

disruption of protein complex means breaking of which bonds

A

H bonds (second, tert, quat structures)

155
Q

structure that has deoxyribose and purine

A

ATP

156
Q

structure that has ribose and pyrimidine

A

UTP

157
Q

more CO2 produced does what to blood

A

lowers pH of blood

158
Q

in the endosymbiotic theory, mitochondria were said to resemble prokaryotic or eukaryotic origin

A

prokaryotic

159
Q

what makes erythrocytes a good model to study plasma membranes

A

their simple structure; no organelles or nucleus

160
Q

at the active site of enzyme, polar molecules are attracted to what molecules on substrate binding site

A

polar; and vice versa for nonpolar

161
Q

at the active site of enzyme, positive charges are attracted to what charges on substrate binding site

A

negative

162
Q

at the active site of enzyme, hydrophobic amino acids attract what on substrate binding site

A

hydrophobic amino acids; and vice versa with hydrophilic

163
Q

where does fatty acid oxidation occur

A

cytoplasm

164
Q

ACTH released by anterior pituitary to increase what hormone production

A

cortisol

165
Q

Complex I of ETC is reduced by what; then it reduces what

A

reduced by NADH; then reduces coenzyme Q

166
Q

Complex II of ETC is reduced by what; then it reduces what

A

reduced by FADH2; then reduces coenzyme Q

167
Q

Complex III is reduced by what; then reduces what

A

reduced by coenzyme Q; then reduces cytochrome c

168
Q

Complex IV is reduced by what; then reduces what

A

reduced by cytochrome c; reduces oxygen

169
Q

in the absence of oxygen, will the amount of acetyl-CoA increase or decrease and why

A

decrease; b/c products of glycolysis will favor lactic acid fermentation

170
Q

at pH of 7, how many protons do carboxylic acids and phosphate groups lose?

A

carboxyl loses 1; phosphate group loses 2 if it has 2 OH’s attached

171
Q

if blood pH is higher, the conc. of what is lower and does acid dissociate?

A

conc. of H+ is lower; but acid will dissociate

172
Q

a gene being continuously expressed is found in hetero or euchromatin?

A

euchromatin

173
Q

fatty acid structure: head and tail

A

head: carboxyl group
tail: long hydrocarbon chain

174
Q

from endo and mesoderm

A

bladder

175
Q

interactions of amino acids w/ OPPOSITE CHARGE where atleast 2 heavy atoms lie within a hydrogen bonding distance

A

salt bridge

176
Q

as pH rises, what usually happens, protonation or deprotonation

A

deprotonation

177
Q

3 monosaccharides to know

A

glucose, fructose (5 membered ring), galactose

178
Q

3 disaccharides to know

A

lactose, sucrose, maltose

179
Q

crumpling proteins up into specific tertiary or quaternary structures does what to water molecules

A

maximizes the freedom of water molecules to move

180
Q

what denatures a protein’s tertiary and quaternary structure?

A

pH; b/c deals with ionic bonds (+ and - charges)

181
Q

what denatures the secondary, tertiary, and quaternary structures of proteins

A

temp, chemicals, and

182
Q

denaturation does not disrupt what structure of a protein?

A

primary

183
Q

alpha helix breakers

A

glycine and proline

184
Q

cysteine is in its reduced form intra or extracellularly

A

intracellularly

185
Q

cystine is in its oxidized form intra or extracellularly

A

extracellularly

186
Q

what amino acid can form a covalently bonded dimer

A

cysteine; disulfide bridge

187
Q

cooperative processes have what shape curve

A

sigmoidal

188
Q

using Native PAGE and SDS-PAGE, how many bands will you see if you use a homodimer and why

A

1 band for both; you would think you would see two b/c its a dimer..but you won’t b/c since it’s “homo”, the two dimers have the same weight and therefore would occupy position of one single band

189
Q

complex formed b/t 2 substrate molecules and an enzyme

A

ternary complex

MCAT (6 decks)

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