test 2: protein structure Flashcards

1
Q

covalent bonds are present in what protein structure level

A

primary

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2
Q

what bonds do secondary protein structure have

A

covalent and hydrogen bonds

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3
Q

what bonds are more prevalent in tertiary and quaternary protein structuer

A

hydrophobic effect

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4
Q

what is significant about covalent bonds in protein strucutre

A
  • shows in amino acid sequence
  • location of s-s bonds
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5
Q

H bonds

A
  • interaction of amino acids close to each other
  • form specific patterns
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6
Q

hydrophobic effect level

A
  • 3d structure of polypeptide
    quat
  • arrangement of multiple folded molecules
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7
Q

what % of DB character does a peptide bond have

A

40

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8
Q

what are the characteristics of a peptide bond

A
  • planar
  • no rotation around peptide bond
  • cis/ trans isomerism
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9
Q

what isoermism are peptide bonds

A
  • nearly 90% are trans
  • 10% are cis
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10
Q

why is trans configuration better than cis

A

steric hinderance and interactions

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11
Q

in peptide bond where can rotation occur

A

around the alpha carbon but there is no rotation at all

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12
Q

what does a ramachandran plot show

A
  • sterically allowed alpha and beta angles for a polypeptide chain
  • limited amount of allowed configurations
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13
Q

2nd protein structure is found where

A
  • local segments of biopolymers
  • proteins and nucleic acids (DNA/ RNA)
  • local conformations
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14
Q

what is an example of a secondary protein structure

A
  • alpha helix
  • beta strnad
  • beta bend
  • collagen triple helix
  • loops and turns
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15
Q

what bonding is present in secondary

A
  • H bonding between backbone amide NH of one AAand the carbonyl of another
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16
Q

who proposed the alpha helix

A

linus pauling

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17
Q

what bonds are present in alpha helix

A
  • h bonds between n and n+4 residue
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18
Q

where do R groups poin on alpha helix

A

outward, perpendicular to the axis

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19
Q

what are some characteristics of alpha helix structure

A
  • h bonds are parallel
  • pitch = 5.4 angstrom
  • 3.6 residue/ turn
    1.5 Rise/AA
  • right hand
    -charged AA
  • dipole polarity
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20
Q

how is alpha helix dipole polarity

A
  • all c=O grpups point toward C and give dipole with + N, (-) C termini
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21
Q

how can you make a stable alpha helix

A
  • end C term with a charged AA to neutralize
22
Q

which protein has predominantly alpha helices

23
Q

what does proline do to alpha helix

A
  • detabilizes the alpha helix that why it is not found
24
Q

do alpha helices like bulky things

25
what are the alpha helix detablilizers
- proline - bulkiness - R groups to large( tryptophan and tyrosine) - too small (glycine)
26
what is an amphipathic helics
hydrophonic residues on one side - hydrophi8llic resides on opposite sides
27
what is keratin
-key structural material in hair skin and nails - coiled coil - 2 amphipathic alpha helices
28
what amino acid is kertatin rich in
- cys to form s-s bonds
29
what does a perm do
- reduce s-s bonds--> 2RSH ; then reoxidize to s-s
30
why is keratin important
used to detect heavy metal poisoning
31
what are B strands
polypeptide chain almost fully extended found in B sheets
32
what is a beta sheet
multiple b strands arranged side by side
33
what are charactersitcs of B strands and B sheets
- h bonds occur between aa on adjacent stands and perp to the strand direction - side chains R-gps alternate in pointing above and below plane perp to b bonds and stands
34
do beta sheets like bulky
yes they do
35
what is an antiparallel b sheet
stand runs in opposite direction
36
parallel
run in the same N to C direction
37
what is the beta sheet structure
- zig zag - 6-12 residue - repeat 2AA distance 7A - may be amphipathic
38
what is silk fibroin
antiparallel B sheets of Gly-ser-gly
39
what does ala do in a silk fibroin
interlocksw/ ala from another sheett
40
what is collagen
- main sturctural protein in the extracellular matrix in connective tissues - most abundant protein in mamels
41
where is collagen present
- bone matrix - tendonds -cartilage - blood vessesl
42
what is the repeating AA in collagen
G-P-P proline helix
43
where are the gly residues located in collagen
- invariant - central axis of triple helix, other can't fit
44
does interchain H bonds occur in collagen
no
45
what helps stabilize the helix
- interchain H bonds w/ Hydroxypro
46
what is osteogenesis imperfecta
- mutation in a gene for collagen - gly is substituted for another AA - prevents normal production of collagen - leads to brittle bones
47
to form hydroxypro what is required
O2 and ascorbic acid(vitamin c)
48
what is scurvy
vitamin c deficiency - lack of hydroxypro - not enough interchain h bonding - tweaking collagen
49
how are collagen fibrils strengthened
- interchain lysine-lysine interaction hydroxypyrindium covalent cross links
50
increase in cross links =
less eslatic collagen= more brittle bones = sign of old age
51
why are loops and turns important
- allow chain reversal - found on the surface of globular protein
52