[Radius of gyration is indicator of compactness of protein structure]

Mol Biol (Mosk). 2008 Jul-Aug;42(4):701-6.
[Article in Russian]


Search and study of the general principles that govern kinetics and thermodynamics of protein folding generate a new insight into the factors controlling this process. Statistical analysis of radii of gyration for 3769 protein structures from four general structural classes (all-alpha, all-beta, alpha/beta, alpha + beta) demonstrates that each class of proteins has its own class-specific radius of gyration, which determines compactness of protein structures: alpha-proteins have the largest radius of gyration. This indicates that they are less tightly packed than beta- and alpha + beta-proteins. Finally, alpha/beta-proteins are the most tightly packed proteins with the least radius of gyration. It should be underlined that radius of gyration normalized on the radius of gyration of ball with the same volume, is independent of the length in comparison with such parameters as compactness and number of contacts per residue.

Publication types

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

MeSH terms

  • Models, Molecular*
  • Protein Folding*
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Thermodynamics


  • Proteins