TY - JOUR
T1 - Nature of driving force for protein folding
T2 - A result from analyzing the statistical potential
AU - Li, Hao
AU - Tang, Chao
AU - Wingreen, Ned S.
PY - 1997/1/1
Y1 - 1997/1/1
N2 - 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.
AB - 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.
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U2 - 10.1103/PhysRevLett.79.765
DO - 10.1103/PhysRevLett.79.765
M3 - Article
AN - SCOPUS:7044220745
SN - 0031-9007
VL - 79
SP - 765
EP - 768
JO - Physical review letters
JF - Physical review letters
IS - 4
ER -