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Biochemistry > Protein Structure > Flashcards

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
Q

shape of a protein is entirely a result of

A

rotation next to chiral carbons

26
Q

all living organisms have _____ handed amino acids

A

left handed, L-amino acids

27
Q

peptide bonds between AA’s are also known as

A

amide bonds

28
Q

tautomerization

A

change in position of lone pair and double bonds to yield two different constitutional isomers

29
Q

resonance

A

change in position of lone pair and double bonds that does not change position of atoms

30
Q

importance of double-bond characteristic of the peptide bond

A

prevents bond rotation between adjacent amino acids
locks peptide into a flat “planar” confirmation

31
Q

phi bonds

A

between alpha carbon and NH2 bond

32
Q

psi bonds

A

between alpha carbon and the COO- group

33
Q

proteins ___________ function as linear polymers

A

DO NOT

34
Q

Aspartate abbreviations

A

aka aspartic acid
Asp
(D)

35
Q

glutamate abbreviations

A

aka glutamic acid
Glu
(E)

36
Q

asparagine abbreviations

A

Asn
(N)

37
Q

glutamine abbreviations

A

Gln
(Q)

38
Q

cysteine abbreviations

A

Cys
(C)

39
Q

lysine abbreviations

A

Lys
(K)

40
Q

arginine abbreviations

A

Arg
(R)

41
Q

serine abbreviations

A

Ser
(S)

42
Q

threonine abbreviations

A

Thr
(T)

43
Q

global protein folding is in reference to what level of protein structure

A

tertiary

44
Q

subunit association is in reference to what level of protein structure

A

quaternary structure

45
Q

enzymes are

A

catalysts

46
Q

regulatory proteins

A

turn things on and off

47
Q

transport proteins

A

facilitate intracellular transport etc

48
Q

storage proteins

A
49
Q

motility proteins

A

move stuff (think flagellin on sperm)

50
Q

structural protiens

A

keratin, cytoskeleton, collagen, etc.

51
Q

scaffold proteins

A

play a role in cellular communication

52
Q

protective proteins

A

antibodies, etc.

53
Q

what types of bonds are responsible for secondary protein structure

A

hydrogen bonds

54
Q

heat _____________ proteins

A

denatures

55
Q

amino acids that can form disulfide bonds contain a ______ group

A

thiol (SH)

56
Q

which amino acids contain sulfur

A

cysteine and methionine

Biochemistry (10 decks)

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