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Protein Structure Flashcards

1
Q

primary proteins

A

directional linear polimers

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2
Q

secondary proteins

A

alpha helix and beta sheets

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3
Q

tertiary structure

A

family of related 3D structures made of alpha and beta helixes

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4
Q

quaternary structures

A

“super structures”, made of multiple combinations

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5
Q

amino acid group attached to the alpha carbon

A

carboxylic acid (COOH)
amino group (NH2)
R-group

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6
Q

Acidic R-groups

A

Aspartic Acid (D)
Glutamic Acid (E)

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7
Q

Basic R-Groups

A

lysine (K)
Arginine (R)

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8
Q

difference between aspartic acid and glutamic acid

A

glutamic acid has additional CH2

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9
Q

lysine structure

A

(CH2)4 NH3+

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10
Q

arginine structure

A
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11
Q

Aspartate (D) pKa

A

3.9

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12
Q

Glutamate (E)

A

4.3

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13
Q

Glutamate (E)

A

4.3

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14
Q

Lysine (K) pKa

A

10.5

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15
Q

arginine (R) pKa

A

12.5

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16
Q

if pH is above the pKa (HH equation)

A

equation favors products

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17
Q

if pH is below the pKa (HH equation)

A

equation favors the reactants

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18
Q

polar amino acids

A

serine
threonine
cysteine
asparagine
glutamine
tyrosine

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19
Q

nonpolar amino acids

A

glycine
alanine
valine
leucine
isoleucine
methionine
phenylalanine
tryptophan
proline

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20
Q

bond between two amino acids

A

peptide bond

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21
Q

aromatic amino acids

A

phenylalanine
tryptophan
tyrosine
histidine*

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22
Q

“structural” amino acids

A

glycine
proline

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23
Q

what is unique about glycine

A

not chiral
no unique R-group, just “H”

24
Q

what is unique about proline

A

side chain “loops back” and forms circle when it bonds with the NH2

25
shape of a protein is entirely a result of
rotation next to chiral carbons
26
all living organisms have _____ handed amino acids
left handed, L-amino acids
27
peptide bonds between AA's are also known as
amide bonds
28
tautomerization
change in position of lone pair and double bonds to yield two different constitutional isomers
29
resonance
change in position of lone pair and double bonds that does not change position of atoms
30
importance of double-bond characteristic of the peptide bond
prevents bond rotation between adjacent amino acids locks peptide into a flat "planar" confirmation
31
phi bonds
between alpha carbon and NH2 bond
32
psi bonds
between alpha carbon and the COO- group
33
proteins ___________ function as linear polymers
DO NOT
34
Aspartate abbreviations
aka aspartic acid Asp (D)
35
glutamate abbreviations
aka glutamic acid Glu (E)
36
asparagine abbreviations
Asn (N)
37
glutamine abbreviations
Gln (Q)
38
cysteine abbreviations
Cys (C)
39
lysine abbreviations
Lys (K)
40
arginine abbreviations
Arg (R)
41
serine abbreviations
Ser (S)
42
threonine abbreviations
Thr (T)
43
global protein folding is in reference to what level of protein structure
tertiary
44
subunit association is in reference to what level of protein structure
quaternary structure
45
enzymes are
catalysts
46
regulatory proteins
turn things on and off
47
transport proteins
facilitate intracellular transport etc
48
storage proteins
49
motility proteins
move stuff (think flagellin on sperm)
50
structural protiens
keratin, cytoskeleton, collagen, etc.
51
scaffold proteins
play a role in cellular communication
52
protective proteins
antibodies, etc.
53
what types of bonds are responsible for secondary protein structure
hydrogen bonds
54
heat _____________ proteins
denatures
55
amino acids that can form disulfide bonds contain a ______ group
thiol (SH)
56
which amino acids contain sulfur
cysteine and methionine

Biochemistry (10 decks)

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