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T2 - BioChem midterm 1 > BC - unit 2 > Flashcards

BC - unit 2 Flashcards

1
Q

___ ___ is a monomeric unit of peptides and proteins

A

amino acids

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2
Q

most amino acids occur as __-__ ___ ___

A

L- alpha amino acids

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3
Q

10 essential amino acids

A 
phenylalanine
valine
threonine
tryptophan
isoleucine
methionine
histidine
arginine
leucine
lysine
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4
Q

3 letter abbreviation of phenylalanine

A

phe

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5
Q

3 letter abbreviation of valine

A

val

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6
Q

3 letter abbreviation of threonine

A

Thr

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7
Q

3 letter abbreviation of tryptophan

A

trp

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8
Q

3 letter abbreviation of isoleucine

A

Ile

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9
Q

3 letter abbreviation of methionine

A

Met

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10
Q

3 letter abbreviation of histidine

A

His

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11
Q

3 letter abbreviation of arginine

A

Arg

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12
Q

3 letter abbreviation of leucine

A

Leu

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13
Q

3 letter abbreviation of lysine

A

Lys

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14
Q

acronym for essential amino acids

A

PRVT TIM HALL

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15
Q

what two essential amino acids can adults synthesize but babies and kids cannot?

A

Histidine

Arginine

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16
Q

12 non-essential amino acids

A 
glycine
alanine
serine
tyrosine
cysteine
aspartic acid
asparagine
glutamic acid
glutamine
proline
hydroxyproline
hydroxylysine
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17
Q

what two non-essential acids are not required for protein synthesis?

A

hydroxyproline

hydroxylysine

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18
Q

5 aliphatic amino acids

A 
Glysine
alanine
valine
leucine
isoleucine
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19
Q

5 hydroxyl amino acids

A 
serine
threonine
tyrosine
hydroxylysine
hydroxyproline
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20
Q

2 sulfer amino acids

A

cysteine

methionine

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21
Q

3 carboxyl/amide amino acids

A

aspartic acid
glutamic acid
asparagine

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22
Q

4 basic amino acids

A

lysine
arginine
histidine
hydroxylysine

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23
Q

4 aromatic amino acids

A

histidine
phenylalanine
tyrosine
tryptophan

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24
Q

2 Pyrrolidine amino acids

A

proline

hydroxyproline

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25
Q

phenylalanine is used to make ___

A

tyrosine

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26
Q

____ is an intermediate of the sulfur –> methianine

A

homocysteine

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27
Q

__ functions with vit B12

A

homocysteine

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28
Q

high levels of homocysteine is associated with ____

A

atherosclerosis

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29
Q

___, __, ___ is used to try and counteract homocysteine to make more cysteine and methianine

A

B6, 9, 12

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30
Q

___, ____, ___ ___ are intermediates in biosynthesis of urea

A

ornithine
citrulline
arginosuccinic acid

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31
Q

_-___ used as a drug for parkinsons disease

A

L-DOPA

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32
Q

L-DOPA is a precursor for biosynthesis of ____

A

catecholamines

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33
Q

3 of the most abundant catecholamines

A

epinephrine
norepinephrine
dopamine

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34
Q

all catecholamines are produced by ___ and ___

A

phenylalanine

tyrosine

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35
Q

____ –> tyrosine –> L-DOPA (catechol) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> norepinephrine –> epinephrine

A

phenylalanine

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36
Q

phenylalanine –> ____ –> L-DOPA (catechol) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> norepinephrine –> epinephrine

A

tyrosine

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37
Q

phenylalanine –> tyrosine –> _____ (___) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> norepinephrine –> epinephrine

A

L-DOPA (catechol)

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38
Q

phenylalanine –> tyrosine –> L-DOPA (catechol)–> ___ (____) –> NO LONGER AN AMINO ACID –> norepinephrine –> epinephrine

A

dopamine (catecholamine)

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39
Q

phenylalanine –> tyrosine –> L-DOPA (catechol) –> dopamine (catecholamine) –> ___ ____ ____ ___ ___ –> norepinephrine –> epinephrine

A

NO LONGER AN AMINO ACID

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40
Q

phenylalanine –> tyrosine –> L-DOPA (catechol) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> ____ –> epinephrine

A

norepinephrine

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41
Q

phenylalanine –> tyrosine –> L-DOPA (catechol) –> dopamine (catecholamine) –> NO LONGER AN AMINO ACID –> norepinephrine –> ___

A

epinephrine

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42
Q

thyroid hormone is deried from ___

A

tyrosine

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43
Q

tyrosine is a precursor to ___

A

thyroxine

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44
Q

2 precursors of thyroid hormone

A

3 - monoiodotyrosine

3,5 - diiodotyrosine

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45
Q

thyroid hormone does 3 things

A

increases basal metabolic rate
protein synthesis
cell proliferation

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46
Q

hyperthyroidism

A

too much thyroxin

increase BMR

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47
Q

increase BMR causes

A 
weight loss
more heat
sensitive to heat
sweating
anxiety
flushing
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48
Q

T4 is ___ abundant than T3

A

more

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49
Q

T4 is ___ active than T3

A

less

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50
Q

_-____ is part of pantothenic acid (Vit B5)

A

beta-alanine

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51
Q

___ is part of taurocholic acid (bile acid)

A

taurine

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52
Q

-chol

A

cholesterol

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53
Q

bile acid is based off ___

A

cholesterol

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54
Q

___ helps with integrity and function of the retina

A

taurine

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55
Q

___ is an inhibitory neurotransmitter from glutamate

A

GABA

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56
Q

___ ___: when the 4 groups on a carbon are different

A

chiral carbon

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57
Q

chiral carbon can deflect ___ ___

A

polarized light

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58
Q

chiral carbons that deflect light to the left are ___ also by __ or __

A

levorotatory
l
-

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59
Q

chiral carbons that deflect light to the right are ___ also by __ or __

A

dextrorotatory
d
+

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60
Q

____: a molecule which possesses both positive and negative charges

A

zwitterion

61
Q

at low pH there will be ___ (+) charge

A

more

62
Q

at high pH there will be ____(-) charge

A

more

63
Q

lot of H+ around ___ and ___ are favored

A

NH3+

COOH

64
Q

low pH: there is lot of ___ in the solution

A

H+

65
Q

if [COO-] is equal to [COOH] then the ration of [COO-]/[COOH] is equal to ___

A

one

66
Q

is the acid form equals the base form then the pH is ___ to the pKa

A

equal`

67
Q

if R-groups are hydrocarbons –> ___

A

hydrophobic

68
Q

hydrophobic amino acids can form ____ bonds

A

hydrophobic

69
Q

___ bonds: association between hydrophobic compounds

A

hydrophobic

70
Q

if R-groups are polar then they are ___

A

hydrophillic

71
Q

hydrophilic amino acids can form ___ or ___ bonds

A

ionic or hydrogen

72
Q

if R groups are aromatic they have strong ___ absorption

A

UV

73
Q

if R groups are -OH they become esterified by ____

A

PO4

74
Q

phosphorylation alters ___ function

A

protein

75
Q

if R groups are SH they can oxidize to form __ bond

A

disulfide

76
Q

if R-groups are SH they maintain a ___ structure

A

tertiary

77
Q

___ bond is between COOH and NH3

A

amide/peptide

78
Q

disulfide bond is usually formed between two ___

A

cysteines

79
Q

disulfide bonds are involved in __ reactions

A

redox

80
Q

if R groups are OH or NH2 they can form ____ by covalently bonding carbs in ___ bonds

A

glycoproteins

glycosidic

81
Q

peptides have ___ than 10 amino acids

A

less

82
Q

polypeptides have __ than 10 amino acids

A

more

83
Q

proteins have ___ amino acids and can be comprised of many ___

A

many

polypeptides

84
Q

amino terminal are always on the ___

A

left

85
Q

carboxy terminal are always on the __

A

right

86
Q

____ is an intracellular antioxidant

A

glutathione

87
Q

glutathione prevents ___

A

oxidation

88
Q

___ can reduce back to what it was before oxidation

A

gluthione

89
Q

if redox happens then ___ has to happen somewhere and vis versa

A

oxidation

90
Q

____ _ is a pain neurotransmitter

A

substance P

91
Q

___ _ is an 11 amino acid peptide in gut, spinal cord and brain

A

substance P

92
Q

___ are vasodilatiing amino acids that are derived from proteolytic cleavage

A

kinins

93
Q

____: analgesic action like opiates

A

opiopeptides

94
Q

3 opiopeptides

A

enkaphalins
beta-endorphin
dynorphin
ALL HAVE -in

95
Q

enkaphalins are ___

A

pentapeptides

96
Q

beta endorphin is a ___ amino acid polypeptide derived from ___

A

30

lipotropin

97
Q

___: an opiopeptide in the spinal cord

A

dynorphin

98
Q

primary structure of proteins are connected by ___ bond which can be hydrolyzed by ___ or boiling

A

peptide

proteases

99
Q

primary structure is dictated by ____ in the ___

A

codons

genes

100
Q

primary structure dictates ___ organization

A

subsequent

101
Q

4 forms of secondary structures

A

alpha-helix
beta-pleated sheet
beta-bending
random coil

102
Q

alpha-helix is like a ___ ___

A

spiral staircase

103
Q

beta-bending has a particular ___

A

kink

104
Q

random coil provides ___

A

elasticity

105
Q

alpha helix and beta pleated sheets have ___ bonding between amino acids

A

hydrogen

106
Q

tertiary structure that have 4 types of bonds

A

hydrogen
ionic
hydrophobic interactions
disulfide

107
Q

quaternary structure is when 1 3D protein is linked with a ___

A

second

108
Q

quaternary structure have 3 types of bonds

A

hydrogen
ionic
hydrophobic interactions

109
Q

hemoglobin are a ___

A

hemoprotein

110
Q

adult hemoglobin HbA are written out

A

alpha 2 beta 2

111
Q

fetal HbF are written out

A

alpha 2 gamma 2

112
Q

__ right handed alpha helices in each alpha subunit

A

8

113
Q

__ right handed alpha helices in each beta subunit

A

7

114
Q

functions of hemoglobin

A

O2 and CO2 transport

buffer

115
Q

hemoglobin acts to neutralize huge ___ differences

A

pH

116
Q

what binds O2 (3)

A

iron
histadine (F8)
histadine (E7)

117
Q

histadine (E7) prevents

A

CO binding

118
Q

R form of hemoglobin binds ___ and T form ___ and binds ___

A

O2
cannot
CO2

119
Q

cooperative allosterism

A

binding of 1st O2 takes the longest, the rest get progressively faster. bc binding O2 changes conformation of other subunits, facilitating further O2 binding

120
Q

myoglobin is a ___

A

hemoprotein

121
Q

myoglobin has ___ polypeptide of 153 amino acids

A

1

122
Q

myoglobin has ___ right handed alpha helices with heme between helices E and F

A

8

123
Q

O2 bound to myoglobin is a reserve for when ___ of tissues is low… it is then released for ___ synthesis

A

pO2

ATP

124
Q

most abundant protein in the body

A

collagen

125
Q

mature ___ is composed of 3 alpha carbon chain subunits

A

tropocollagen

126
Q

___ is the most abundant amino acid in collagen, with lots of ___ and ___

A

glycine
proline
lysine

127
Q

collagen synthesis:

mRNA to ___ chain

A

pro-alpha

128
Q

collagen synthesis:
hydroxylation of pro-alpha chains
- proline by ___ ___
- lysine by ___ ____

A

prolyl hydroxylase

lysyl hydroxylase

129
Q

Collagen synthesis:

hydroxylation of proline and lysine require 3 things

A

vitamin C
Iron
O2

130
Q

collagen synthesis:

3 hydroxylated pro-alpha-chains H bond to form __-___

A

pro-collagen

131
Q

___ ___: genetic mutation where gly is replaced by ___

A

cysteine

132
Q

collagen synthesis:

secretion of pro collagen out of cell by ___

A

exocytosis

133
Q

cleavage of N and C terminal segments by procollage peptidases –> ____

A

tropocollagens

134
Q

oxidation of some lysines to ___ ___ by ___ ___ and requires 3 things

A 
lysyl aldehydes
lysyl oxidase
copper
vit B6
O2
135
Q

____ due to defiiciency of lysyl oxidase

A

lathyrism

136
Q

___ formed from condensation of 3 lysine aldehydes + 1 unmodified lysine

A

desmosine

137
Q

desmosine is the marker of ___ ___

A

elastin metabolism

138
Q

rigor mortis happens bc of lack of ___

A

ATP

139
Q

water soluble proteins are ___

A

albumins

140
Q

dilute salt solution proteins are ___

A

globulins

141
Q

acid/base soluble proteins are ___

A

glutelins

142
Q

acid/salt soluble proteins are __

A

basic proteins

143
Q

globular proteins

A

most belong here

144
Q

fibrous proteins

A

elongated

actin, myosin, collagen, elastin, keratin

145
Q

___ proteins: no attachment of non-protein component

A

simple

146
Q

___ protein: apoprotein + prosthetic group = holoprotein

A

conjugated proteins

147
Q

apoprotein is a __ protein

A

naked

148
Q

5 conjugated proteins

A 
hemo
glyco
lipo
phospho
metallo

T2 - BioChem midterm 1 (5 decks)

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