Lecture 2: Elements of protein structure I Flashcards

1
Q

What are the properties of the alpha-helix?

A
  • right turning helical structure with 3.6 amino acids per turn
  • amino acid side chains point outwards - causes polarity
  • optimises hydrogen bonding btw the carbonyl oxygen and the amide
  • 5.4 A pitch
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2
Q

What are the properties of the Beta-sheet?

A
  • arrangement of side chains gives it a pleated look
  • sheets are parallel and antiparallel, they are twisted, NOT flat
  • amino acid side chains point above & below
  • There is hydrogen bonding btw adjacent peptides chains —–> strands
  • Runs from N to C
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3
Q

How is the alpha-helix formed?

A
  • formed from angled H bonds being formed btw the H of an amino acids with a O from another along the spiral
  • n + 4
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4
Q

How is the beta-sheet formed?

A

The beta sheet is formed from the alteration of the directions of the amino acid side chains to eventually form B pleated sheets of amino acids
—> gives it a pleated look

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5
Q

How are side chains orientated in

  • alpha-helix?
  • beta-sheet?
A
a = point outwards
b = above and below
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6
Q

What are beta turns in proteins?

A

They are regions of proteins which have a sudden turn in the chain which:
- allow polypeptide chains to change direction
- found btw strains of antiparallel
Turns are caused by proline and glycine

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7
Q

What is the importance of rotation angles Phi & psi in polypeptide chains?

A

Rotations of Phi & Psi would cause side chains of amino acids in a polypeptide chain to collide as:

  • Phi rotation can lead to O - O collision
  • Psi rotation can lead to NH- NH collision
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8
Q

What are Ramachandram plots? What do they do?

A
  • plots predict the rotation angles which are allowed around an alpha carbon
  • collisions for each amino acids & rotations that avoid steric hindrance were recorded
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9
Q

What is the primary structure of a protein?

A

The order in which amino acids are linked via peptide bonds

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10
Q

What is the secondary structure of a protein?

A

Regions of regular peptide folding stabilised by hydrogen bonds e.g a-helix, b-sheet

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11
Q

What is the tertiary structure?

A

The 3-dimensional arrange of atoms in the protein

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12
Q

What is the quaternary structure?

A

The way in which several polypeptide chains associate in a multi-subunit protein

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13
Q

What is the common amino acid bond rotation?

A

X - amino acid side chain bond angles are called X and are usually staggered to avoid steric hindrance

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