Calculation of the free energy of association for protein complexes

Protein Sci. 1992 Jan;1(1):169-81. doi: 10.1002/pro.5560010117.

Abstract

We have developed a method for calculating the association energy of quaternary complexes starting from their atomic coordinates. The association energy is described as the sum of two solvation terms and an energy term to account for the loss of translational and rotational entropy. The calculated solvation energy, using atomic solvation parameters and the solvent accessible surface areas, has a correlation of 96% with experimentally determined values. We have applied this methodology to examine intermediates in viral assembly and to assess the contribution isomerization makes to the association energy of molecular complexes. In addition, we have shown that the calculated association can be used as a predictive tool for analyzing modeled molecular complexes.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Capsid / ultrastructure
  • Databases, Factual
  • Macromolecular Substances
  • Mathematical Computing
  • Models, Chemical*
  • Protein Conformation*
  • Protein Folding
  • Proteins / chemistry*
  • Rhinovirus / ultrastructure
  • Solubility

Substances

  • Macromolecular Substances
  • Proteins