Nature of Driving Force for Protein Folding: A Result From Analyzing the Statistical Potential

Hao Li, Chao Tang, and Ned S. Wingreen
Phys. Rev. Lett. 79, 765 – Published 28 July 1997
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Abstract

In a statistical approach to protein structure analysis, Miyazawa and Jernigan 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 Miyazawa-Jernigan 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.

  • Received 5 December 1996

DOI:https://doi.org/10.1103/PhysRevLett.79.765

©1997 American Physical Society

Authors & Affiliations

Hao Li, Chao Tang, and Ned S. Wingreen

  • NEC Research Institute, 4 Independence Way, Princeton, New Jersey 08540

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Vol. 79, Iss. 4 — 28 July 1997

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