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

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

1995-12-14

arxiv.org/abs/cond-mat/9512111v2

Phys. Rev. Lett. 79 (1997) 765

Physics

Condensed Matter

Statistical Mechanics

Revised version. 4 pages, Latex

Scientific paper

10.1103/PhysRevLett.79.765

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.

Affiliated with

Also associated with

No associations

Rating

Nature of Driving Force for Protein Folding -- A Result From Analyzing the Statistical Potential does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Nature of Driving Force for Protein Folding -- A Result From Analyzing the Statistical Potential, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Nature of Driving Force for Protein Folding -- A Result From Analyzing the Statistical Potential will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-651391