Nature of driving force for protein folding: A result from analyzing the statistical potential

Hao Li, Chao Tang, Ned S. Wingreen

Research output: Contribution to journalArticle

183 Scopus citations

Abstract

In a statistical approach to protein structure analysis, Miyazawa and Jernigan (MJ) derived a 20×20 matrix of inter-residue contact energies between different types of amino acids. Using the method of eigenvalue decomposition, we find that the MJ matrix can be accurately reconstructed from its first two principal component vectors as Mij=C0+C1(qi+qj)+C2qiqj, with constant C’s, and 20 q values associated with the 20 amino acids. This regularity is due to hydrophobic interactions and a force of demixing, the latter obeying Hildebrand's solubility theory of simple liquids.

Original languageEnglish (US)
Pages (from-to)765-768
Number of pages4
JournalPhysical review letters
Volume79
Issue number4
DOIs
StatePublished - Jan 1 1997

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)

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