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Fundamentals Block 2 > protein structure and function > Flashcards

protein structure and function Flashcards

1
Q

what determines the properties of proteins?

A

side chains

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2
Q

which type of amino acids are proteins composed of?

A

L

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3
Q

What are the nonpolar amino acids?

A

glycine
alanine
valine
leucine
isoleucine
phenylalanine
tryptophan
methionine
proline

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4
Q

what are the uncharged polar amino acids?

A

serine
threonine
tyrosine
asparagine
glutamine
cysteine

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5
Q

what are the acidic amino acids?

A

aspartate
glutamate

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6
Q

what are the basic amino acids?

A

histidine
lysine
arginine

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7
Q

Asp, D

A

aspartate

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8
Q

Glu, E

A

glutamate

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9
Q

His, H

A

histidine

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10
Q

Lys, K

A

Lysine

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11
Q

Arg, R

A

arginine

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12
Q

Ser, S

A

serine

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13
Q

Thr, T

A

threonine

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14
Q

Tyr, Y

A

Tyrosine

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15
Q

Asn, N

A

Asparagine

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16
Q

Gln, Q

A

Glutamine

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17
Q

Cys, C

A

Cysteine

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18
Q

Gly, G

A

Glycine

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19
Q

Ala, A

A

Alanine

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20
Q

Val, V

A

Valine

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21
Q

Leu, L

A

leucine

22
Q

Ile, I

A

Isoleucine

23
Q

Phe, F

A

Phenylalanine

24
Q

Trp, W

A

Tryptophan

25
Q

Met, M

A

methionine

26
Q

Pro, P

A

Proline

27
Q

which amino acids play an important role in buffering changes in physiological pH?

A

Histidine and Cysteine

28
Q

where are nonpolar amino acids found in a protein?

A

interior, membrane proteins

29
Q

where are polar amino acids found in a protein?

A

the surface of soluble proteins

30
Q

primary structure

A

the order of amino acids in the protein

31
Q

what type of bonds form peptide bonds?

A

covalent

32
Q

why is rotation around the alpha carbon limited?

A

steric hindrance (except for gly)

33
Q

what amino acid forms disulfide bonds due to their thiol groups?

A

cysteine

34
Q

secondary structure

A

local structures formed by interactions of amino acid chains

35
Q

alpha helix

A

stabilized by hydrogen bonds involving peptide backbone CO and NH
-sidechains project outward
-3.4 amino acids per turn

36
Q

which amino acids are not found in an alpha helix?

A

-proline breaks the helix by introducing a bend
-glycine is too floppy

37
Q

beta sheet

A

-peptide chains form bonds with neighbors
-stabilized by hydrogen bonds involving peptide backbone CO and NH
-side chains outward
-chains can run parallel or antiparallel

38
Q

unstructured polypeptide is referred to as ________________

A

random coil

39
Q

motifs/supersecondary structures

A

-formed by aggregation of alpha helices, beta sheets
-beta barrels and sandwiches are common structural motifs

40
Q

tertiary structure

A

-overall structure of a protein or subunit
-motifs condense to form domains and entire protein subunits-protein folding

41
Q

when do polypeptides begin to fold into secondary structure?

A

as soon as they are translated

42
Q

where does protein folding occur?

A

cytoplasm and ER
-often assisted by chaperones/heat shock proteins

43
Q

what stabilizes higher order structures?

A

interactions involving side chains

44
Q

delta G/free energy

A

must be negative for reaction to be spontaneous
deltaG=deltaH - TdeltaS

45
Q

delta H/enthalpy

A

energy consumed/released as heat but forming/breaking bonds
-charge charge interactions are highly favorable
-energy is released when salt bridges form
-delta H is negative

46
Q

delta S/entropy

A

-disorder in system
-everything tends toward chaos

47
Q

what drives protein folding in aqueous solutions?

A

positive entropy due to freeing water/hydrophobic effect

48
Q

what can denature protein structure?

A

-chemical agents
-heat
-cold
-(disrupts the hydrophobic effect maintaining the folded state)

49
Q

quaternary structure

A

-interactions of individual proteins or subunits within a functional complex
-can be composed of multiple subunits
-ex. hemoglobin or actin

50
Q

which amino acids can be phosphorylated?

A

serine, threonine, tyrosine

51
Q
A

Fundamentals Block 2 (10 decks)

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