The interrelationships of side-chain and main-chain conformations in proteins

Prog Biophys Mol Biol. 2001;76(1-2):1-102. doi: 10.1016/s0079-6107(01)00005-0.


The accurate determination of a large number of protein structures by X-ray crystallography makes it possible to conduct a reliable statistical analysis of the distribution of the main-chain and side-chain conformational angles, how these are dependent on residue type, adjacent residue in the sequence, secondary structure, residue-residue interactions and location at the polypeptide chain termini. The interrelationship between the main-chain (phi, psi) and side-chain (chi 1) torsion angles leads to a classification of amino acid residues that simplify the folding alphabet considerably and can be a guide to the design of new proteins or mutational studies. Analyses of residues occurring with disallowed main-chain conformation or with multiple conformations shed some light on why some residues are less favoured in thermophiles.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Crystallography, X-Ray / methods
  • Peptides / chemistry
  • Protein Conformation*
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Recombinant Proteins / chemistry
  • Structure-Activity Relationship


  • Peptides
  • Proteins
  • Recombinant Proteins