Lecture 6 Flashcards

1
Q

Why are proteins important?

A
  • mediate nearly all of the processes in a cell
  • they have diverse structure and function
  • all proteins use the same set of 20 amino acids
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2
Q

Name few different types of protein

A
  • enzymes
  • motor proteins
  • signal proteins
  • transport proteins
  • structural proteins
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3
Q

Describe the primary structure of protein

A
  • amino acid sequence
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4
Q

What are amino acids

A
  • amino acids are building blocks of protein
  • all 20 amino acids have similar structure, differing in their side chain (R) which dictates their behaviour
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5
Q

Amino acids can be grouped into 4 categories which are

A
  1. non polar
  2. polar (uncharged)
  3. acidic
  4. basic
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6
Q

what are the basic amino acids

A
  • Arginine
  • Lysine
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7
Q

what are the acidic amino acids

A
  • aspartic acid
  • glutamic acid
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8
Q

Name an uncharged polar amino acid

A
  • serine
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9
Q

Name a non polar amino acid

A
  • valine
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10
Q

What are peptides

A

2+ amino acids joined by peptide bonds which were formed as a result of a condensation reaction

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11
Q

What is each side of a peptide labelled as?

A
  • peptides have directionality with an amino acid terminus (N-terminus) on one side and a carboxyl terminus (C-terminus) in the other
  • it is written from left to right
  • N terminus to C terminus
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12
Q

peptides bonds are found between what

A
  • peptides bonds are found between carbonyl carbon and nitrogen
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13
Q

What dictates the shape of a protein

A
  • the specific amino acid sequence
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14
Q

what dictates how the protein folds

A
  • the side chain
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15
Q

What is the secondary structure of a protein

A
  • stable arrangements of amino acids
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16
Q

Name 2 stable secondary structures

A
  • the a helix
  • the b sheet
17
Q

The a helix

A
  • peptide backbone wraps around imaginary axis
  • 3.6 residues/turn
  • r-group face outwards
  • stabilized by hydrogen bonds
18
Q

how are a helices stabilized by H-bonds

A
  • stabilized by intrachain hydrogen bonds between C double bond O group of each residue with N-H group of amino acids 4 residues away on the polypeptide chain backbone
19
Q

what affects the stability of a helices

A
  1. electrostatic or steric interactions between adjacent side chains can affect the stability of an a-helix
  2. electrostatic or steric interactions between amino acids 3-4 residues away can affect the stability of an a-helix
  3. proline and glycine are usually not found in helices
    - the nitrogen of proline is in a rigid ring which interferes statically with the backbone
    - proline in a peptide bond is missing an amide hydrogen to form hydrogen bonds
    - glycine is very flexible and allows for conformations that aren’t suitable for a helices
    - glycine is so small so it can’t protect the backbone hydrogen bonds from the aqueous environment
20
Q

side chains affect protein _________

A

localization

21
Q

amphipathic helices

A
  • one side is hydrophobic residues and the other side is hydrophilic residues. Allowing for membrane separation
  • helices with a region of hydrophobic residues flanked by hydrophilic residues can allow for membrane spanning
22
Q

what is a protein with a helices

A
  • a keratin
  • forms coiled coils which gives it strength
23
Q

what are B sheets

A
  • composed of B strands
  • stabilized by intrachain hydrogen bonds
  • B sheets can be parallel or anti parallel depending on orientation of strands
24
Q

Parallel B-sheets

A
  • strands run zig zag in the same direction
  • hydrogen bonds connect each amino acid on one strand with two different amino acids on the adjacent strand
25
Q

anti-parallel B sheets

A
  • strands run zig zagged in opposite direction
  • hydrogen bonds connect each amino acid on one strand to one different amino acid on the adjacent strand
26
Q

what are some B sheet properties

A
  • B sheets can be twisted
  • R groups are perpendicular from the plane of the sheet
27
Q

Give an example of a B sheet

A
  • silk fibroin
28
Q

When can B sheet be found in transmembrane

A
  • only if they are a part of the B barrel structure
  • hydrophobic side chains line the outer surface of the b barrel