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biochem > quiz 2 > Flashcards

quiz 2 Flashcards

1
Q

what does protein do

A

perform biochemical functions
catalyzed biochemical reactions

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2
Q

define protein

A

workhorse of life
made of amino acids by peptide bonds

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3
Q

how many amino acids are ionize

A

7

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4
Q

what groups make up an amino acid

A

amino group, carboxyl group, hydrogen, side chain

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5
Q

which amino acid is not chiral

A

glycine

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6
Q

which aminos are negative at pH 7

A

asp and glu

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7
Q

which aminos are positive at pH7

A

lys, arg, leu, asn, gln

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8
Q

which aminos are hydrophilic

A

ser, thr, cys

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9
Q

which aminos are hydrophobic

A

gly, ala, pro, val, leu, ile, met

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10
Q

which aminos are aromatic

A

phe, tyr, trp

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11
Q

name this amino

A

glycine
gly
g

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12
Q

name this amino

A

alanine
ala
a

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13
Q

name this amino

A

valine
val
v

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14
Q

name this amino

A

leucine
leu
L

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15
Q

name this amino

A

isoleucine
ile
I

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16
Q

name this amino

A

proline
pro
p

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17
Q

name this amino

A

methionine
met
m

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18
Q

name this amino

A

phenylalanine
phe
F

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19
Q

name this amino

A

tryptophan
trp
w

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20
Q

name this amino

A

tyrosine
tyr
Y

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21
Q

name this amino

A

serine
ser
s

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22
Q

name this amino

A

threonine
thr
T

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23
Q

name this amino

A

cysteine
cys
C

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24
Q

name this amino

A

aspartic acid
asp
D

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25
Q

name this amino

A

glutamic acid
glu
E

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26
Q

name this amino

A

asparagine
asn
n

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27
Q

name this amino

A

glutamine
gln
Q

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28
Q

name this amino

A

histadine
his
h

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29
Q

name this amino

A

histadine
his
h

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30
Q

name this amino

A

lysine
lys
k

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31
Q

name this amino

A

arginine
arg
R

32
Q

describe primary structure

A

amino acid sequence

33
Q

describe secondary structure

A

3D arrangements of polypeptide backbone

34
Q

describe tertiary structure

A

folding and arrangement of secondary structures

35
Q

describe quarternary structure

A

3D arrangement of separate polypeptide chains

36
Q

what can primary structure be broken into

A

protease or peptidase

37
Q

define residue

A

individual aminos in peptide chain

38
Q

describe the 4 steps of enzyme catalysts

A

enzyme is available and empty
substrate binds to enzyme
substrate converts to product
products are released

39
Q

define net charge

A

overall charge, depends on pH

40
Q

define isoelectric point (pI)

A

average pH where molecule has no electric charge

41
Q

define zwitterion

A

electroneutral molecule containing positive and negative charge

42
Q

what is the equation of pI

A

(pKa1+pKa2)/2

43
Q

what are the 7 ionizable groups

A

asp
glu
his
cys
tyr
lys
arg

44
Q

describe proteins

A

flexible
noncovalent
always in motion
conformational changes

45
Q

what are primary structures stabilized by

A

covalent bonds

46
Q

what are the 3 secondary structures

A

a-helix
B-sheet
B-turn

47
Q

describe a-helix

A

right-handed
3.6 residues per turn
contain n to n+4 H bonds

48
Q

what are the side chain effects

A

interacts together
3-4 residues away
can be charged
bulkiness can cause steric hindrance

49
Q

what is the helix breaker

A

proline

50
Q

what makes a bad helix

A

glycine

51
Q

helix has a…

A

overall dipole movement

52
Q

what are amphiphatic helices used for

A

gating and fat hydrolysis

53
Q

describe B-strand

A

extended polypeptide
side chain above and below backbone
an arrow pointing to C-term

54
Q

describe B-sheet

A

side by side strands with H bonding
backbone is made of of N,H,O
can be parallel or antiparallel

55
Q

describe B-turn

A

2 adjacent segments of antiparallel B-sheets
4 residues long

56
Q

what allows for secondary structure to be possible

A

phi and psi rotation

57
Q

what makes up phi

A

C’, N, Ca, C’

58
Q

what makes up psi

A

N, Ca, C’, N

59
Q

what are the factors of phi and psi

A

steric interference
H-bonding is maximized
with side chains, the phi angle of proline locks in

60
Q

define rhamachandran plots

A

plots all phi and psi in a protein

61
Q

what are the two main types of tertiary structures

A

globular
fibrous

62
Q

describe globular proteins

A

spherical
soluble in H2O
hydrophobic core hydrophilic exterior

63
Q

describe fibrous proteins

A

rod-shaped
insoluble in H2O

64
Q

define domain

A

separate structural units of a protein

65
Q

define desaturation

A

unfolding a protein

66
Q

define renaturation

A

refolding a proteim

67
Q

define disulfide

A

2 cysteine residues that interact after oxidation
a type of cross linking

68
Q

what do enzymes do

A

catalyze rxns by lowering activation energy and increasing the rate of product formation

69
Q

what do structural proteins do

A

maintains cell structure and allows it to change shape
forms polymers

70
Q

what are examples of structural protein

A

actin
tubulin
collagen

71
Q

what do cell signaling proteins do

A

transmit signals

72
Q

describe nuclear receptors

A

regulate gene expression in response to ligand bonding

73
Q

describe intracellular signaling proteins

A

molecular formation changes due to incoming signals

74
Q

describe genomic caretaker proteins

A

maintain accessibility to genomic information
DNA repair, replication, recombination, and gene expression

75
Q

describe transport protein

A

move molecules within and between cells
in plasma membrane
permit polar and charged molecules to pass

76
Q

describe passive transport

A

energy independent
down the concentration gradient

77
Q

describe active transport

A

requires energy (from ATP hydrolysis and ionic gradient)
up the concentration gradient

biochem (11 decks)

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