Thermodynamics of protein folding: a microscopic view.
Statistical thermodynamics provides a powerful theoretical framework for analyzing, understanding and predicting the conformational properties of biomolecules. The central quantity is the potential of mean force or effective energy as a function of conformation, which consists of the intramolecular energy and the solvation free energy. The intramolecular energy can be reasonably described by molecular mechanics-type functions. While the solvation free energy is more difficult to model, useful results can be obtained with simple approximations. Such functions have been used to estimate the intramolecular energy contribution to protein stability and obtain insights into the origin of thermodynamic functions of protein folding, such as the heat capacity. With reasonable decompositions of the various energy terms, one can obtain meaningful values for the contribution of one type of interaction or one chemical group to stability. Future developments will allow the thermodynamic characterization of ever more complex biological processes.
Lazaridis
Themis
T
Department of Chemistry, City College of New York, Convent Ave & 138th Street, New York, NY 10031, USA. themis@sci.ccny.cuny.edu
Karplus
Martin
M
D000465:Algorithms; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003627:Data Interpretation, Statistical; D004735:Energy Transfer; D006801:Humans; D008956:Models, Chemical; D008968:Molecular Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry; D012995:Solubility; D013816:Thermodynamics
D011506:Proteins