peptide stuctures Flashcards
How many amino acid chains make aup a protein
normally 1 however can be many (these make up at Quaternary strcture)
Define the 4 stages of protein structures
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
what are the three parts of the main chain amino acid + properties within these sections
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)
What are the bond angle posibilitys of psi phi and omega
Phi and Psi = +,- 180 degrees
Omega = 0 (cis), 180 (trans) due to planar config of peptide
Why is rotation around phi and psi bonds restricted
Steric hinderance
Phi can cause O-O collision
Psi can cause NH-NH collisions
name the characteristics of the peptude bond
- trans config
- planar sp2 max pi bond
- dipoled (+NH, -Ve C=O)
- 80Kj/mol rot barrier
- 40% double bond characteriest
When is it a peptide bond more linkly to be cis than normal
Bonds preceeding a proline have a 10 % chance to be cis
What are the properties of an alpha helix
- 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
What can the helix wheel view help with
Determining the properties of an alpha helix, where groups of particular side chains are located
- each side chain is seperated by 100 degrees
What is a beta sheet + properties
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
How do beta sheets look
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
What are the key properties of turns
- 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
What is the acepted 3d structure model for proteins
Ribbon model/ Richardson model
- alpha helix shown as spirals, beta sheets as arrows from N-C, turns + coils shown as loop like structures