Open AccessProtein model structure evaluation using the solvation free energy of folding.
Author(s) -
Laurent Chiche,
Lydia M. Gregoret,
Fred E. Cohen,
Peter A. Kollman
Publication year - 1990
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.87.8.3240
Subject(s) - solvation , protein folding , folding (dsp implementation) , downhill folding , implicit solvation , chemistry , folding funnel , lattice protein , crystallography , correctness , chemical physics , thermodynamics , computational chemistry , phi value analysis , molecule , physics , computer science , biochemistry , organic chemistry , electrical engineering , programming language , engineering
A systematic study of solvation free energy of folding for proteins with known crystallographic structures is presented. There is a linear relationship between the solvation free energy of folding and the protein size. This relationship, which can be rationalized by a simple model of chain folding, allows prediction of the solvation free energy of folding for proteins for which no high resolution structures are available. All misfolded structures analyzed show solvation free energies higher than predicted; however, some of the misfolded structures have values close enough to the predicted values so that one must be very careful when using such a criterion to check the correctness of a protein model.