GENERALLY the Ramachandran plot originally
developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V.
Sasisekharan, is a way to visualize energetically allowed regions
for backbone dihedral angles ψ against φ of amino acid residues in
protein structure.
- The one might be expect that larger side chains would result in
more restrictions and consequently a smaller allowable region in
the Ramachandran plot.
- In exercise, the major effect seen is that of the presence or
absence of the methylene group at Cβ. Glycine has only a hydrogen
atom for its side chain, with a much smaller van der Waals radius
than the CH3, CH2, or CH group that starts
the side chain of all other amino acids.
- From now it is least restricted, and this is apparent in the
Ramachandran plot for glycine for which the allowable area is
considerably larger.
- In gap, the Ramachandran plot for proline, with its
5-membered-ring side chain connecting Cα to backbone N, shows a
limited number of possible combinations of ψ and φ
- A large set of high-resolution structures and outlines for
favored and for allowed conformational regions for the general case
(all amino acids except Gly, Pro, and pre-Pro), for Gly, and for
Pro.The most common regions are labeled: α for α helix, Lα for
lefthanded helix, β for β-sheet, and ppII for polyproline II.