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

Abstract

In a statistical approach to protein structure analysis, Miyazawa and Jernigan (MJ) derived a $20\times 20$ 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 $M_{ij}=C_0+C_1(q_i+q_j)+C_2{q}_i{q}_j$, 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.

Revised version. 4 pages, Latex

References in corpus (2)

• Freezing Transition of Random Heteropolymers Consisting of an Arbitrary Set of Monomers
• Random Hydrophilic-Hydrophobic Copolymers

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