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BMSC 200 > Module 4 > Flashcards

Module 4 Flashcards

1
Q

what are peptide bonds

A

covalent linkages between carboxyl + amino group of 2 separate amino acids

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2
Q

what is the repeating pattern of polypeptide main chains?

A

NCCNCC

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3
Q

what is primary structure?

A

linear sequence of amino acids
N-> C terminus

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4
Q

what is the primary structure pattern?

A

YGGFL

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5
Q

what is ramachadran plots?

A

illustrate possible configurations of phi + psi

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6
Q

what is the secondary structure?

A

localized folding within polypeptide

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7
Q

how is secondary structure maintained?

A

H+ bonds between main chain amide + carbonyl groups

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8
Q

what are the 2 key rules of secondary structure?

A
  1. optimize potential
  2. represent a favoured configuration
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9
Q

why are hydrogen acceptors/donors important in secondary structure?

A

for optimization

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10
Q

how are PHI bonds attached to alpha carbons?

A

on the N terminus

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11
Q

how are PSI bonds attached to alpha carbons?

A

on the C terminus
think “C for Psi”

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12
Q

what are the 2 characteristics of Alpha Helices?

A
  1. right handed
  2. have 3.6 residues per turn
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13
Q

what 4 amino acids are not found in alpha helices?

A
  1. proline
  2. glycine
  3. amino acids with side branches
  4. amino acids with H+ groups near main chain
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14
Q

why is proline not found in alpha helices?

A

its too rigid

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15
Q

why is glycine not found in alpha helices?

A

too flexible

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16
Q

what charge does the N terminus carry?

A

partial positive charge with negative residues (asp, glu)

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17
Q

what charge does the C terminus carry?

A

partial negative charge with positive residues

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18
Q

what are beta sheets made of?

A

4 or 5 B strands arranged side by side

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19
Q

configuration of B sheets?

A

fully extended polypeptide chain

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20
Q

true or false: antiparallel beta sheets are more stable than parallel sheets

A

true, they have better alignment of H+ donors + acceptors

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21
Q

what are mixed beta sheets?

A

both parallel + antiparallel strands

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22
Q

what is the pattern of side chains in amphipathic B sheets?

A

alternating pattern above & below polypeptide chain, they attach polar face to the non-polar face

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23
Q

what is denaturation?

A

adding heat to a protein to disrupt structure (is reversible)

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24
Q

what is tertiary structure?

A

the final folding pattern of a single polypeptide

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25
Q

what is native confirmation of tertiary structure?

A

biological active folding pattern

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26
Q

true or false: primary structure dictates tertiary structure

A

true

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27
Q

what is stability?

A

tendency to maintain native conformation

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28
Q

what does stability reflect?

A

the difference in free energy of folded/unfolded states

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29
Q

what amount of free energy is most stable?

A

lowest free energy

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30
Q

2 characteristics of folded proteins?

A
  1. low energy state
  2. greatest stability
31
Q

is protein folding a slow or rapid process?

A

rapid

32
Q

what are chaperones?

A

heat shock proteins that help the protein perform complex functions

33
Q

why are chaperones often called heat shock proteins?

A

b/c they are induced by shock

34
Q

what are quaternary structures?

A

subset of proteins

35
Q

how are quaternary structures formed?

A

when 4 subunits non-covalently join together and create a binding site

36
Q

what are 3 advantages of quaternary structure?

A
  1. stability
  2. produce active sites
  3. produce complex combinations
37
Q

how big are proteins?

A

100-1000 amino acids in length

38
Q

at 51 amino acids ( ) is used as a threshold of when a polypeptide becomes a protein

A

insulin

39
Q

what is the smallest protein?

A

insulin

40
Q

what is the largest protein?

A

Titin

41
Q

how to calculate the number of amino acids a protein has?

A

molecular weight / 110

42
Q

what is the most important force & why?

A

non-covalent b/c they stabilize structure

43
Q

what are fibrous proteins?

A

simple proteins that hold your body together

44
Q

what are the 3 fibrous proteins?

A
  1. keratin
  2. collagen
  3. Silk
45
Q

what are Globular Proteins?

A

proteins that perform highly complex functions & structures

46
Q

role of hemoglobin

A

transporting O2 in bloodstream

47
Q

role of myglobin

A

storage of O2 in the lungs

48
Q

what is keratin?

A

primary component in hair, nails & horns

49
Q

what does a pseudo trend mean in keratin?

A

positions a & d are hydrophobic residues

50
Q

where is the hydrophobic strip located in keratin?

A

along the length of the helix

51
Q

what are keratin coiled coils?

A

when 2 amphipathic keratin helices put their hydrophobic faces together

52
Q

when are coiled coils formed?

A

when 2 or more helices entwine to form a stable structure

53
Q

what are the 2 reasons for coiled coils?

A
  1. greater strength
  2. greater durability
54
Q

what kind of helices are involved in keratin coiled coils?

A

2 right handed wrapped to the left

55
Q

what is post translational stabilization?

A

covalently modified structures through the use of disulphide bonds

56
Q

how much protein does collagen make up in the body?

A

25%

57
Q

where is collagen found?

A

skin, tendons & vascular system

58
Q

primary structure of collagen

A

GLY-X-Y pattern (X is often proline)

59
Q

1/3 of residues in collagen is ( ) and the other 1/3 is ( )

A

glycine and proline

60
Q

how many residues per turn does collagen have?

A

3

61
Q

how are collagen coiled coils formed?

A

when 3 left handed helices join together & wrap to the right

62
Q

where are proline side chains located on collagen coiled coils?

A

on the outside

63
Q

what is post-translational modification in collagen?

A

occur from hydroxyproline & hydroxylysine

64
Q

what vitamin is required for collagen post-translational modifcation?

A

vitamin C, is needed for stable crosslinks

65
Q

What is silk’s primary structure?

A

has a 6 residue repeat (GSGAGA)

66
Q

what is silk’s secondary structure?

A

beta sheets

67
Q

what is the strongest silk material?

A

cross sectional

68
Q

what do fully extended polypeptide chains give?

A

strength

69
Q

what does association of strands by hydrogen bonding allow for?

A

flexibility

70
Q

what 2 amino acids come together & form a zipper?

A

alanine & glycine

71
Q

is silk non-immuniogenetic or immunogenetic?

A

non-immuniogenetic

72
Q

what does non-immuniogenetic mean?

A

when the body can recognize the molecule has not itself and provokes an immune response

73
Q

what is a steric interference

A

2 groups cannot occupy the same space at the same time

BMSC 200 (10 decks)

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