Calculation of the free energy of association for protein complexes

Nancy Horton, Mitchell Lewis

Research output: Contribution to journalArticle

313 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)169-181
Number of pages13
JournalProtein Science
Volume1
Issue number1
DOIs
StatePublished - Jan 1992
Externally publishedYes

Keywords

  • hydrophobicity
  • protein structure
  • solvation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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