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BMSC 200 > Chapter 4 > Flashcards

Chapter 4 Flashcards

1
Q

average molecular weight of an amino acid

A

110

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2
Q

How do you approximate the number of amino acids in a protein?

A

dividing the proteins molecular weight by 110.

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3
Q

smallest protein

A

insulin: ~50

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4
Q

biggest protein

A

titin

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5
Q

The 3D structure of a protein is determined by…

A

its amino acid sequence

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6
Q

the most important forces stabilizing the specific structures of a given protein are…

A

non-covalent

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7
Q

low free energy means…

A

most stable

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8
Q

Folded proteins occupy a….

A

low-energy state

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9
Q

Protein folding _________ the order.

A

increases

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10
Q

denaturation

A

loss of activity; reversible (energy required is small)

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11
Q

Folding and unfolding is a ______________ process

A

cooperative

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12
Q

cooperative process

A

as soon as some come apart, it all comes apart

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13
Q

Within main-chain of the polypeptide, there is a repeating pattern of…

A

NCCNCC

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14
Q

To represent a viable form of secondary structure, the folding pattern must:

A
  • optimize the hydrogen bonding potential of main chain carbonyl and amide groups
  • represent a favoured conformation of the polypeptide chain
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15
Q

There are _____ numbers of hydrogen bond donors and accepts within the polypeptide main chain.

A

equal

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16
Q

most residues within biological peptides and proteins tend to be in….

A

trans configuration

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17
Q

Trans configuration can’t convert to cis without….

A

breaking bonds

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18
Q

Each alpha carbon is held within the main chain through…

A

single bonds with complete freedom of rotation

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19
Q

Phi

A

alpha carbon to amide nitrogen

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20
Q

Psi

A

alpha carbon to carbonyl carbon

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21
Q

Ramachadran Plot

A

Illustrates all possible combos of Phi and Psi

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22
Q

alpha helices are ______ handed helices

A

right

23
Q

right handed helix

A

3.6 residues/turn

24
Q

alpha helices are stabilized by..

A

many hydrogen bonds which are parallel to helix axis

25
Q

All C=O groups point towards….

A

C-terminus

26
Q

Which amino acids are usually not found in alpha helices?

A

proline and glycine

27
Q

Stretches of similarly charged residues will ________ alpha helices due to ______________.

A

destabilize, electrostatic repulsion

28
Q

The positioning of hydrophobic and hydrophilic residues with primary structure generates…..

A

an amphipathic alpha helices

29
Q

conformation of beta strands

A
  • fully extended polypeptide chains

- side chains projected alternately above and below

30
Q

How are beta strands stabilized ?

A

by hydrogen bonds between C=O and -NH on adjacent strands

31
Q

Which are more stable, parallel or anti-parallel beta sheets?

A

anti

32
Q

Unique _______ produced at the interfaces between subunits of quaternary structure.

A

active sites

33
Q

Keratin primary structure

A

-pseudo seven repeat (a and d are hydrophobic)

34
Q

Keratin secondary

A

right handed, amphipathic alpha helices

35
Q

keratin tertiary

A

the hydrophobic strip in alpha helical rods are looking for hydrophobic environment

36
Q

keratin quaternary structure

A

hydrophobic surfaces interact to form coiled coils

37
Q

coiled coil of keratin

A

-two right-handed helices wrapping in a left-handed fashion

38
Q

Individual units of keratin are linked together through…

A

disulfide bonds

39
Q

What determines overall strength of keratin?

A

extent of disulfide bonds

40
Q

collagen makes up…

A

tendons, skin

41
Q

collagen primary

A

multiple repeats of Gly-X-Y where X is often proline or hydroxyproline

42
Q

collagen secondary

A

-formations of left handed helices (3 residues/turn)

43
Q

collagen tertiary

A

full length helical

44
Q

quaternary

A

coiled coils

45
Q

coiled coils of collagen

A

three left handed helices wrapping in right handed fashion

46
Q

What determines strength of collagen?

A

linkages from amino acid residues that undergo post-translational modification

47
Q

The enzyme that performs performs the stabilizing links (involving p.t.m residues) of collagen require….

A

VITAMIN C

48
Q

silk primary

A

six residue repeat (GSGAGA)

49
Q

silk secondary

A

composed primarily from beta sheets (strength)

50
Q

silk is both flexible and strong because…

A
  • fully extended polypeptide chains (strength)
  • beta sheets (flex)
  • association of sheets by van der Waals and hydrophobic interactions (flex)
51
Q

Hydrogen bonds hold….

A

beta sheets together (non-covalent)

52
Q

hydrophobic and van der Waal interactions bring ________ together

A

beta sheets

53
Q

Entire helix is a dipole with N (__) and C (__).

A

N=+

C= -

BMSC 200 (11 decks)

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