peptide stuctures Flashcards

1
Q

How many amino acid chains make aup a protein

A

normally 1 however can be many (these make up at Quaternary strcture)

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2
Q

Define the 4 stages of protein structures

A

Primary - the aminoa acid sequence
secodary - The short stuctures formed by adjacent sections of amino acids
tertiary - the 3d sturcture of an amino acid chain
Quatinary - the interchain packing of multiple proteins

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2
Q

what are the three parts of the main chain amino acid + properties within these sections

A

Amino N, alpha carbon Ca, Carboxy carbon C’
flexibilty between bonds
between N + Ca = Phi (Φ)
between Ca and C’ = Psi (Ψ)
Between C’ -> N (peptide) = omega (ω)

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3
Q

What are the bond angle posibilitys of psi phi and omega

A

Phi and Psi = +,- 180 degrees
Omega = 0 (cis), 180 (trans) due to planar config of peptide

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4
Q

Why is rotation around phi and psi bonds restricted

A

Steric hinderance
Phi can cause O-O collision
Psi can cause NH-NH collisions

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5
Q

name the characteristics of the peptude bond

A
  • trans config
  • planar sp2 max pi bond
  • dipoled (+NH, -Ve C=O)
  • 80Kj/mol rot barrier
  • 40% double bond characteriest
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6
Q

When is it a peptide bond more linkly to be cis than normal

A

Bonds preceeding a proline have a 10 % chance to be cis

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7
Q

What are the properties of an alpha helix

A
  • Right handed spiral around central axis, N- > C
  • H-Bond stabilised between n, n+4 residues between C=O and N-H
  • each H-bond has 12-28Kj/mol every to stabilise
  • 3.6 residues per turn rising 5.4A
  • side chains point outwards
  • dipols act in the same direction in the helix
  • Glycine + proline break alpha helix structure
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8
Q

What can the helix wheel view help with

A

Determining the properties of an alpha helix, where groups of particular side chains are located
- each side chain is seperated by 100 degrees

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8
Q

What is a beta sheet + properties

A

Made up from adjacent beta strands which H-bond to one annother
make a beta sheet 2-10 strands thick and 6-15 amino acids long
often have P-NP-P-NP… squence

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9
Q

How do beta sheets look

A

betasheets have a right handed twist,
they are pleated structures
Can run parralel with V shaped H-bonds or
antiparralel with perpendicular H-bonds
they have alternating top bottom side chains

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10
Q

What are the key properties of turns

A
  • form globular proteins
  • hairpin loops often 3-4 residues
  • often contain glycine or proline
  • 30% of protein residue
  • common to have H-bond across turn
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11
Q

What is the acepted 3d structure model for proteins

A

Ribbon model/ Richardson model

  • alpha helix shown as spirals, beta sheets as arrows from N-C, turns + coils shown as loop like structures
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