amino acids and proteins Flashcards

(46 cards)

1
Q

basic structure of amino acids

A

nh3 group
central carbon
cooh group
hydrogen

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2
Q

all amino acids are

A

L- amino acids

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3
Q

what kind of organisms have d amino acids

A

bacteria

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4
Q

which orientation are most amino acids? R/s?

A

most are S with the exception of cystine

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5
Q

what is the R/S configuration of cysteine

A

R

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6
Q

aliphatic amino acids

A

G, A, V, L, I, P

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7
Q

is methionine polar or nonpolar

A

nonpolar

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8
Q

what is unique about proline?

A

it disrupts secondary protein stucture and causes proline kinks

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9
Q

which amino acids can be phosphorylated

A

serine, threonine, tyrosine on their -OH residues

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10
Q

what is unique about histidine?

A

pka of 6.0 so it acts as a buffer at physiological pH

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11
Q

amide amino acids

A

glutamine (Q) asparagine (N)

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12
Q

sulfur containing amino acids

A

cysteine and methionine

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13
Q

which amino acids are achiral

A

glycine only

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14
Q

peptide bond

A

hydrolysis reaction that takes the OH group from a COOH and the next H from an NH3 group

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15
Q

proteases

A

hydration reaction that breaks up primary structure/ breaks the peptide bonds

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16
Q

average protein size

A

50 kDa

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17
Q

how are proteins assembled in the ribosome

A

from the N to C terminus

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18
Q

terciary structure

A

interactions are typically non-covalent and charge driven.
- salt bridges
- disulfide bridges

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19
Q

2- mercatoethanol

A

a reducing agent that breaks up disulfide bonds

20
Q

what kind of bond are disulfide bridges

A

COVALENT
- very strong compared to most tericiary interactions

21
Q

where does hydrogen bonding occur in secondary structure of proteins

A

between the COOH anf NH3 residues of the protein backbone

22
Q

what structure do proteases cleave

23
Q

what structure do denaturing agents cleave?

A

2, 3, 4
- not permenent

24
Q

taq polymerase

A

a protein that is challenging to denature at high temp and is used in PCR technique

25
entropy relationship with protein folding
proteins will fold in a way that encourages entropy, so it is considered favorable - example: why hydrophobic tail is on side of lipid bilayer
26
zwitterion
ion where one group of amino acid is negative (coo-) and 1 is positive (nh3+) - so for normal amino acid at physiological ph charge is 0
27
henderson - hasselbach eqn
pH = pKa + log [A-/HA]
28
pKa
pH= -log[H+]
29
pka
point where half of a functional group is positive and half is 0
30
when pka> pH
not abundant amounts of h+ in solution so functional group is deprotinated
31
when pka
plentiful h+ in solution and species is protinated
32
pka1
cooh, around 2.3
33
pka2
nh3 around 9.5
34
isoelectric point pI
pH where average charge is 0
35
isoelectric point for diprotic amino acids
average pka1 and pka2
36
isolelectric point for triprotic amino acids that are acidic
pka1 + pkar / 2 (two acidic)
37
isolelectric point for triprotic basic amino acids
pka2 + pkar / 2 (2 basic
38
flat region of a titration curve
pka and half of species is prot/ deprot -buffer zone
39
vertical region of a titration curve
isoelectric point
40
ph = pka
half equivalence point
41
equivalence point
isoelectric point = pH - the middle of the vertical region where charge is 0
42
what stabilizes a peptide bond
resonance between c=o bond and makes the bond unable to rotate bc of planar
43
stecker synthesis
making amino acids from aldehydes via 1. imine 2. add cyanide (form nitrile) 3. hydrolysis to form cooh
44
imine group
C=N where n has 1 or 2 R groups
45
nitrile group
c triple bond N
46
precursor to gabriel synthesis
N-pththalidicmalonic ester "THAD" - use nitrogen for amine group - central c and cooh