Lecture 2 Flashcards

1
Q

nuclear proteins

A

RNA, DNA

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2
Q

immunoglobulin example

A

antibody

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3
Q

invader that causes the immune response

A

antigen

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4
Q

proteins are made of

A

amino acids

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5
Q

L amino acid and D amino acid are blank

A

mirror images (stereoisomers)

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6
Q

molecule with both + and - charges

A

zwitterions

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7
Q

molecule that acts as acid base

A

ampholyte

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8
Q

charged ends of amino acids form blank bond

A

peptide

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9
Q

peptide bond aka blank bond

A

amide

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10
Q

two amino acids are joined with the accompanying loss of a water molecule

A

condensation reaction

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11
Q

condensation reaction is catalyzed by the blank

A

ribosome

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12
Q

water inhibits blank

A

protein synthesis

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13
Q

end terminus of peptide chain

A

carboxyl

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14
Q

terminus of peptide chain that is at the beginning

A

amino group

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15
Q

number of R group options…. R groups are amino acids in proteins

A

20

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16
Q

two cysteines can react together to form a strong covalent blank bond

A

disulphide

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17
Q

proteins are purified to be used in

A

drugs

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18
Q

gel electrophoresis distributes and purifies proteins according to blank

A

charge

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19
Q

small proteins migrate blank in gel electrophoresis

A

fast

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20
Q

ion exchange does not usually fully blank proteins

A

purify

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21
Q

size exclusions has blank getting through first

A

large

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22
Q

sds gel electrophoresis separates by size and allows large proteins through blank than smaller

23
Q

proton donor

24
Q

proton acceptor

25
strong acids and bases blank in water
dissociate completely
26
weak acids make good blank because they dissociate blank in water
buffers, incompletely
27
the larger Ka, the blank the tendency for the acid to dissociate
greater
28
large Ka means blank acid
strong
29
strong acid means a blank pKa
small
30
pKa = -(log10) Ka
henderson hasselbeck
31
Ka of a weak base is actually a measure of the dissociation a proton from its blank
conjugate acid
32
measure of ionizable species in a solution
titration curve
33
pH at which the net charge on species is zero on average
isoelectric point
34
at blank, 50% protonated 50% unprotonated
pKa
35
solution pH higher than the pKa of amino acid, then amino acid is blank
deprotonated
36
solution pH lower than the pKa of amino acid, then amino acid is blank
protonated (has all its protons)
37
net charge of protein is the blank of all ionic species
mean
38
henderson hasselbeck equation
pH = pKa + log (products/reactants)
39
a buffer is a weak acid or base and a blank of that weak acid or base
salt
40
biological buffers funciton
maintain homeostasis
41
2 carriers of oxygen proteins
hemoglobin, myoglobin
42
straight or branched CHn chain
aliphatic
43
nonpolar small aliphatic aa
gly, ala
44
Nonpolar, aliphatic (bulky)
VAL, LEU, ILE
45
Branched-chain
VAL, ILE, LEU, ARG, ASN, GLN
46
Aromatic
PHE, TYR, TRP
47
Charged, acidic (negative)
ASP, GLU
48
Charged, basic (positive)
HIS, LYS, ARG
49
Polar, uncharged, amides
ASN [--> ASP], GLN [--> GLU]
50
Polar, uncharged, hydroxy
TRY, SER, THR
51
Polar, uncharged, sulfur-containing
MET, CYS
52
only amino acid that is not optically active
glycine
53
very hydrophobic aromatics
phenylalanine, Tryptophan... not tyrosine because of hydroxyl group
54
blank side chains act as buffers at physiological pH
histidine