Polymers of Life 5: Proteins Flashcards

1
Q

definition of alpha amino acid

A
  • Molecules that contain an amino group and a carboxylic acid group that are separated by 1carbon
  • carbon atom next to the COOH group ( therefore no. 2 in carbon chain staring from that functional group ) is called the alpha carbon dioxide
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2
Q

What does alpha amino acid’s naming usually start with

A

2-amino

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3
Q

What is an amino acid

A
  • amine group NH2
  • carboxylic acid
  • R group
  • H
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4
Q

What happens when you join amino acids together

A

polypeptides are formed with the removal of water due to it being a condensation reaction

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5
Q

How would you describe a peptide bond

A

A covalent bond that is rigid and cannot turn

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6
Q

How would you describe different polypeptide

A
  • Backbone of polypeptides is generally the same but with different R groups attached
  • R groups will affect the shape of the polypeptide due to R groups being different sizes
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7
Q

Describe a primary structure of a protein

A

Sequence of amino acids which is unique to each protein

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8
Q

Describe secondary structure of a protein

A
  • coiling & folding of the polypeptide because of hydrogen bonds into an alpha helix and a beta sheet

( - Spatial arrangement of sections of primary structure e.g. helixes or sheets

  • held together by hydrogen bonds )
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9
Q

Describe tertiary structure of a protein

A

Overall 3-D shape of protein Based on interactions between its various side chains

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10
Q

Why is the sequence of amino acids not random

A

It is determined by genetic information DNA

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11
Q

What is shapes kind of secondary structure of a protein take shape in

A
  1. Alpha helix = held together by hydrogen bonds be

2. beta pleated sheet = held together by hydrogen bonds between amide + carbonyl group

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12
Q

And a polypeptide folds in on itself from a secondary to tertiary what kinds of intermolecular forces are responsible for holding it together
( 4 )

A
  1. Ionic bonds = NH3+ and COO- of exposed amino acids ( due to zwitterion form of amino acids )
  2. Hydrogen bonds = amide + carbonyl groups or alcohols
  3. instantaneous dipole - induced dipole = non polar side chains ( large hydrocarbon groups )
  4. Disulphide bridges = covalent bonds between amino acid cysteine which includes sulphur atoms
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13
Q

Describe the strength of the four intermolecular forces holding protein structures together

A

Srongest

  • disulphide bridges
  • hydrogen bonding
  • ionic bonds
  • instantaneous dipole - induced dipole

Weakest

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14
Q

Describe the levels of organisation of a protein

A
  1. Primary = Sequence of amino acids of the protein
  2. Secondary = Hydrogen bonds in the peptide chain back pain = alpha helix and beta sheets
  3. Tertiary = Mostly in noncovalent interactions between that our groups within the protein
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15
Q

Describe haemoglobin

A
  • Protein that carries oxygen and red blood cells
  • 4 polypeptide chains = 2 identical alpha chains & 2 identical beta chains

= overall quaternary structure due to 2 secondary structures ( alpha & beta ) coming together

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