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MCAT 1 > Biochemistry > Flashcards

Biochemistry Flashcards

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1
Q

steps of the gabriel synthesis

A

deprotonation to anion
addition of R-Br
amide hydrolysis to a di-carboxyl

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2
Q

L

A

Leucine

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3
Q

cysteine

A

Cys

C

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4
Q

secondary structure

A

alpha helicies and beta sheets

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5
Q

immune system proteins

A

antigens and antibodies

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6
Q

are the R groups parallel or perpendicular in beta sheets

A

perpendicular

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7
Q

mannose

A

C6H12O6

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8
Q

negatively charged amino acids

A

aspartic acid

glutamic acid

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9
Q

sugars with the formula C3H6O3

A

glyceraldehyde

dihydroxyacetone

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10
Q

isomerases

A

rearrangements

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11
Q

charge below the isoelectric point

A

positive

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12
Q

Glycine

A

Gly

G

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13
Q

what is the preferred model of enzyme specificity

A

induced fit

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14
Q

what proton is donated first from an amino acid

A

COOH

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15
Q

R

A

arginine

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16
Q

characteristics of amino acids

A

alpha carbon stereocenter

absolute configuration

R group chemistry

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17
Q

C

A

cysteine

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18
Q

minerals

A

inorganic molecules essential for bone formation

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19
Q

isoelectric point of basic amino acid

A

amine and R group

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20
Q

galactose

A

C6H12O6

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21
Q

glutamic acid

A

Glu

E

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22
Q

can enzymes become saturated

A

yes

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23
Q

x intercept of lineweaver burke plots

A

-1/Km

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24
Q

T

A

threonine

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25
Q

ligases

A

large molecule synthesis

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26
Q

cell adhesion molecules are an example of

A

binding protein

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27
Q

isoprene

A

C5H8 with one C=C double bond on the end and one attached to C3

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28
Q

peptide bond formation

A

dehydration synthesis and acyl substitution

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29
Q

what enantiomer is found in the human body

A

D

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30
Q

what direction do amino acids flow

A

N –> C

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31
Q

what filaments are present in actin

A

thin and microfilaments

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32
Q

non-reducing sugar example

A

sucrose

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33
Q

charge above the isoelectric point

A

negative

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34
Q

sucrose

A

glucose+fructose

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35
Q

pka of acidic R groups

A
  1. 7 Asp

4. 5 Glu

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36
Q

lock and key model

A

active site of an empty enzyme is an exact fit for the substrate

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37
Q

terpenes

A

mostly conjugated unsaturated polymer of isoprene

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38
Q

polysaccharides

A

Cn(H2O)x

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39
Q

tertiary structure

A

geometric 3D folding on alpha helicies and beta sheets to form a globular/ structural protein

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40
Q

V

A

valine

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41
Q

isoelectric point of neutral amino acid

A

amine and carboxyl pKa

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42
Q

how is competitive inhibition overcome

A

increasing substrate concentration

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43
Q

pka of basic R groups

A

10.7 Lys

12 Arg

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44
Q

where does proline occur in an alpha helix

A

often the first residue, not found within the helix

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45
Q

what type of isomers are glucose and galactose

A

epimers

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46
Q

alpha linkages

A

linked through oxygen on the opposite plane from CH2OH

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47
Q

lipids

A

hydrophobic biomolecules

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48
Q

asparagine

A

Asn

N

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49
Q

monosaccharides

A

(CH2O)n

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50
Q

molten globule

A

partially folded

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51
Q

what is fibroin and what secondary structure does it have

A

silk

beta sheets

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52
Q

are coenzymes permanently attached to an enzyme

A

no

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53
Q

conjugated protein

A

associated with cofactors by covalent or intermolecular forces

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54
Q

what linkages attach a triacylglycerol

A

ester linkages

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55
Q

what are kinesins and dyneins used for

A

vesicles, cell division, cilia and flagella

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56
Q

mixed inhibition

A

inhibitor has unequal affinity for ES and E, favoring one over the other

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57
Q

lactose

A

glucose and galactose

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58
Q

what is keratin and what secondary structure does it have

A

found in hair and nails

alpha helix

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59
Q

transferases

A

functional group transfer

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60
Q

nonpolar amino acids

A 
proline
glycine 
alanine
valine
leucine
isoleucine
methionine
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61
Q

intramolecular nucleophilic substitution

A

ring closing reaction

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62
Q

how does competitive inhibition change Km

A

increases

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63
Q

H

A

histidine

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64
Q

isoelectric point separation

A

uses a gel with a stable pH gradient and protein moves through an increasing pH and will stop moving when pH is equal to pI

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65
Q

does the non-competitive inhibitor show preference for ES or E?

A

neither

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66
Q

beta glucose

A

OH up

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67
Q

how does mixed inhibition change Km

A

decreases when ES increases over E

increases when E increases over ES

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68
Q

isoelectric point

A

pH when a molecule has no net charge

[pka(1)+pka(2)]/2

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69
Q

are vitamins organic

A

yes

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70
Q

hydrolases

A

hydrolysis

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71
Q

how does competitive inhibition change Vmax

A

unchanged

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72
Q

M-M saturation curve

A

graph of reaction velocity versus substrate concentration

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73
Q

characteristics of an active site

A

contains amino acids that will associate with the substrate

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74
Q

triacylglycerol

A

glycerol backbone attached to r chain

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75
Q

are the positive amino acids acidic or basic?

A

basic

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76
Q

what filaments are present in tubulin

A

microtubules

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77
Q

solvation layers

A

layer of water surrounds a dissolved protein interaction with one another and the protein surface

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78
Q

oxidoreductases

A

redox reactions

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79
Q

example of positive cooperativity

A

hemoglobin

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80
Q

feedback inhibition

A

negative feedback

inhibition that applies to a multi-step synthetic pathway where a product later in the chain acts as an inhibitor for an enzyme in an earlier step

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81
Q

two protein separation techniques

A

isoelectric point

electrophoresis

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82
Q

are the R groups directed into or out of the helix

A

out of

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83
Q

how does mixed inhibition change Vmax

A

decreases

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84
Q

how many residues occur between alpha helicies

A

four

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85
Q

S

A

serine

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86
Q

strecker synthesis

A

aldehyde with NH3 and HCN add cyano and NH2 to the C

Add hydrogen ions and water for the amino acid

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87
Q

what type of isomers are D and L

A

enantiomers

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88
Q

positively charged amino acids

A

arginine
histidine
lysine

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89
Q

glycogen

A

alpha linkages, branched

animals

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90
Q

autocrine

A

self-target

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91
Q

substrate

A

molecule acted upon by an enzyme

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92
Q

quaternary structure

A

association of multiple folded proteins into a multi-subunit complex

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93
Q

salt bridges

A

acidic and basic R groups go through neutralization reactions resulting in salt formation

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94
Q

when is Km equal to [S]

A

half of Vmax

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95
Q

oligopeptide

A

small chain of amino acids

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96
Q

non-competitive inhibition

A

inhibitor binds away from the active site and changes the enzyme shape

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97
Q

triacylglycerol is the same as

A

triglycerides

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98
Q

transcription factors are an example of

A

binding protein

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99
Q

sulfur linkage

A

S-S between cysteines

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100
Q

I

A

isoleucine

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101
Q

are the negative amino acids acidic or basic?

A

acidic

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102
Q

forms of tertiary structure (6)

A 
hydrogen bonding 
disulfide bonds 
hydrophobic/hydrophilic interactions
ionic interactions
van der waals interactions 
proline turns
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103
Q

lineweaver burke plots

A

double inverse plot of reaction rate (1/v) versus substrate concentration (1/[S])

104
Q

Vmax

A

rate of reaction at saturation levels of substrate, theoretical maximum velocity

105
Q

serine

A

Ser

S

106
Q

cofactors

A

metal ions or small molecules that assist in catalysis

107
Q

are prosthetic groups permanently attached to an enzyme

A

yes

108
Q

what type of isomers are alpha and beta glucose

A

anomers

109
Q

tryptophan

A

Trp

W

110
Q

fatty acid

A

carboxyl attached to an R chain

111
Q

proline

A

Pro

P

112
Q

how are vitamins acquired

A

diet

113
Q

fat soluble vitamins

A

A D E K

114
Q

does a lower or higher pka lose a proton?

A

lower

115
Q

positive feedback

A

product of reaction acts as an agonist to activate a receptor

116
Q

arginine

A

Arg

R

117
Q

histidine

A

His

H

118
Q

what is the electrophile in an intramolecular nucleophilic substitution

A

Carbon with carbonyl

119
Q

active site

A

section of the enzyme where the substrate is converted to product

120
Q

methionine

A

met

M

121
Q

glycolipids

A

sugars attached to lipids

122
Q

reversible enzyme inhibition

A

inhibitor is not permanently bound and the enzyme is not completely disabled

123
Q

ribose

A

C5H10O5

124
Q

sphingolipid

A

fatty acid derivatives of shingosine

125
Q

lysine

A

Lys

K

126
Q

how does non-competitive inhibition change Vmax

A

decreases

127
Q

positive cooperativity

A

ligand affinity increases with the binding of each subsequent ligand

128
Q

tryosine

A

Tyr

Y

129
Q

what filaments are present in elastin

A

connective tissue

130
Q

protein folding

A

hydrophobic r groups fold into the core and hydrophilic are common on the surface

131
Q

structural proteins

A

actin, tubulin, keratine, elastin

132
Q

cellulose

A

beta linkages

plants

133
Q

calmodulin is an example of

A

binding protein

134
Q

what is the pka of a strong acid

A

lower

135
Q

hemoglobin is an example of

A

binding protein

136
Q

Km

A

michaelis constant

relative measure of an enzyme’s affinity for substrate

137
Q

y intercept of lineweaver burke plots

A

1/Vmax

138
Q

competitive inhibition

A

inhibitor binds at active site, inhibitor resembles substrate

139
Q

initial velocity is equal to

A

[VmaxS]/[Km+S]

140
Q

agonist

A

activates a receptor to a response

141
Q

simple protein

A

contains only amino acids and no non-protein cofactors

142
Q

uncompetitive inhibition

A

inhibitor binds only to the enzyme-substrate complex

143
Q

lysases

A

cleavage

144
Q

L configuration

A

OH on the left

145
Q

enzyme-substrate complex

A

formed when the substrate is bound in the activated site and the substrate is catalyzed to product

146
Q

G

A

glycine

147
Q

molten

A

fully unfolded, denatured

148
Q

deoxyribose

A

C5H10O4

149
Q

alpha glucose

A

OH down

150
Q

induced fit

A

active site changes as the substrate binds, increases affinity for the substrate and for the transition state (lowers Ea)

151
Q

examples of lipids

A

fats, oils, waxes, steroids, glycerides

152
Q

alpha helicies

A

hydrogen bonding between the carbonyl O and amide H

153
Q

what are the exceptions of the L/S configuration of amino acids

A

glycine (not chiral)

cysteine

154
Q

disulfide bonds

A

two oxidized cysteine residues (R-S-S-R)

between alpha helicies in keratin makes hair curly or straight

155
Q

pka of NH3+

A

9

156
Q

how does non-competitive inhibition change Km

A

unchanged

157
Q

are minerals organic

A

no

158
Q

is an enzyme or a general catalyst faster

A

enzyme

159
Q

apoenzyme

A

simple enzyme

160
Q

what charge will a protein have in a pH below the pI

A

positive charge

161
Q

aspartic acid

A

Asp

D

162
Q

are saturated or unsaturated molecules healthier

A

unsaturated

163
Q

ketose

A

from a ketone

164
Q

K

A

lysine

165
Q

glutamine

A

Gln

Q

166
Q

A

A

alanine

167
Q

M

A

methionine

168
Q

where are waxes found

A

coatings on leaves and stems

169
Q

michaelis menten kinetics

A

M-M

170
Q

hydrophobic core

A

hydrophobic R groups fold into the interior of a globular protein to escape water

171
Q

troponin is an example of

A

binding protein

172
Q

saponification

A

hydrolysis of an ester using KOH into a glycerol and an acid

173
Q

what is the difference between kinesins and dyneins

A

direction

kinesins move from - to +, from the center to the periphery in a cell, from nerve to dendrite

174
Q

how does uncompetitive inhibition change Km

A

decreases

175
Q

pka of histidine

A

6

176
Q

fructose

A

C6H12O6

177
Q

glyceraldehyde

A

C3H6O3

178
Q

Proteins

A

amino acid polymers

179
Q

aldose

A

from an aldehyde

180
Q

irreversible inhibition

A

inhibitor binds covalently to the enzyme and active site disabling the enzyme for a prolonged period of time, or permanently

181
Q

leucine

A

Leu

L

182
Q

is cellulose digestible by humans

A

no

183
Q

D

A

aspartic acid

184
Q

P

A

proline

185
Q

how does uncompetitive inhibition change Vmax

A

increases

186
Q

what does the strecker synthesis create

A

alpha-aminonitriles

187
Q

glucose

A

C6H12O6

188
Q

paracrine

A

immediate vicinity

189
Q

zwitterion

A

+ and - functional groups cancel one another out

@ pH of 7.4 the COOH is COO- and NH2 is NH3+

190
Q

polypeptide

A

longer chain of amino acids

191
Q

what type of isomers are epimers

A

diastereomers

192
Q

Valine

A

Val

V

193
Q

deoxy

A

-OH is replaced by H

194
Q

E

A

glutamic acid

195
Q

beta linkages

A

linked through oxygen on the same plane as CH2OH

196
Q

linkages used to attach glycolipids

A

glycosidic bond

R-O-CH2 of glycerol backbone

197
Q

what linkages attach lactose

A

beta

198
Q

what is the configuration of almost all amino acids

A

L and S

199
Q

exceptions to zwitterion at pH of 7.4

A

charged R groups

200
Q

allosteric enzymes

A

activity is influenced by the reversible, non-covalent binding of another molecule

201
Q

maltose

A

glucose+glucose

202
Q

reducing sugar

A

can reduce a free aldehyde or ketone group

all monosaccharides

203
Q

what is the strongest type of protein folding interactions?

A

disulfide bonds

204
Q

what is the nucleophile in an intramolecular nucleophilic substitution

A

OH on the chiral C

205
Q

phenylalanine

A

Phe

F

206
Q

isoleucine

A

Ile

I

207
Q

are enzymes universal

A

no, specific

208
Q

hydrophilic surface

A

surface R groups are polar or charged

209
Q

polar amino acids

A 
serine
threonine
cysteine
asparagine
gluamine
210
Q

electrophoresis

A

separate based on size with the smallest traveling the farthest

211
Q

what does mercaptoethanol do

A

reduce disulfide bonds

212
Q

F

A

Phenylalanine

213
Q

what is Km inversely proportional to?

A

E-S binding affinity

214
Q

zymogen

A

inactive enzyme precursor that when activated, converts to the active form

215
Q

beta sheets

A

hydrogen bonding beween the carbonyl O and amide H

216
Q

how to irreversibly denature a protein

A

heat

217
Q

where do resonance bonds form in a protein

A

carbonyl and nitrogen

218
Q

why are zymogens important

A

important for enzymes needed quickly but that would be detrimental if active at all times

219
Q

Y

A

tyrosine

220
Q

N

A

asparagine

221
Q

aromatic amino acids

A

phenylalanine
tryptophan
tyrosine

222
Q

motor proteins

A

myosin, kinesins/dyneins

223
Q

where does proline occur in a beta sheet

A

at the end to enable the 180° shift to the next row

224
Q

electrostatic interactions

A

interactions between charged R groups

225
Q

dihydroxyacetone

A

C3H6O3

226
Q

starch

A

alpha linkages, branched

plants

227
Q

vitamins

A

relatively small, organic molecules that are essential nutrients for metabolism

228
Q

globule

A

fully folded

229
Q

steroids

A

4 membered ring structures

230
Q

phospholipids

A

polar head group (phosphate) attached to a triacylglycerol

231
Q

protein denaturing agents

A

acid
heat
urea
mercaptoethanol

232
Q

isoelectric point of acidic amino acid

A

R and carboxyl pKa

233
Q

alanine

A

ala

A

234
Q

furanose

A

5 carbons

235
Q

D configuration

A

OH on the right

236
Q

holoenzyme

A

enzyme and cofactors

237
Q

waxes

A

ester of a long-chain (12-32 C) alcohol and a fatty acid

fatty acid-ester-alcohol

238
Q

where are sphingolipids found

A

cell membrane of brain and nervous tissue

239
Q

are enzymes organic or inorganic

A

organic

240
Q

mercaptoethanol structure

A

HS-C-C-OH

241
Q

sugars with the formula C6H12O6

A

glucose
fructose
galactose
mannose

242
Q

what do alpha-aminonitriles do

A

intermediates in amino acid synthesis

243
Q

residues

A

amino acids

244
Q

prostaglandins

A

lipid mediators that have autocrine and paracrine functions in the body

245
Q

example of a steroid

A

cholesterol

246
Q

pyranose

A

6 carbon

247
Q

what filaments are present in keratin

A

intermediate filaments

248
Q

primary structure

A

amino acid sequence

249
Q

pka of COOH

A

2

250
Q

Threonine

A

Thr

T

251
Q

Q

A

glutamine

252
Q

what charge will a protein have in a pH above the pI

A

negative charge

253
Q

what is myosin used for

A

cellular transport

254
Q

histones are an example of

A

binding protein

255
Q

W

A

tryptophan

MCAT 1 (10 decks)

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