Thermodynamics protein folding

Privalov, P. L., and Makhatadze, G. I., 1993. Contributions of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration. y(9wra z/ of Molecular Biology 232 660-679. 

Shakhnovich H. I. Theoretical studies of protein-folding thermodynamics and kinetics. Curr. Op. Str. Biol. (1997) 7(1) 29-40. 

Makhatadze GI, Privalov PL. Contribution of hydration to protein folding thermodynamics. 1. The enthalpy of hydration. J. Mol. 34. Biol. 1993 232 639-659. 

Shakhnovich EL Protein Folding thermodynamics and dynamics where physics, chemistry, and biology meet. Chem. Rev. 2006 106 1559-1588. 

A. Cooper, Heat capacity of hydrogen-bonded networks an alternative vievt> of protein folding thermodynamics, in Biophys. Chem., 2000, 85, 25-39. 

Eugene I. Shakhnovich, Protein Folding Thermodynamics and Dynamics where Physics, Chemistry, and Biology Meet , Chemical Reviews, v. 106, pp. 1559-1588, 2006. 

E. I. Shakhnovich, Curr. Opin. Struct. Biol., 7, 29 (1997). Theoretical Studies of Protein-Folding Thermodynamics and Kinetics. 

The techniques listed above are dynamical simulations. It is also possible to use bead interaction potentials for strictly thermodynamic calculations. For example, the following steps have been used for protein-folding problems ... 

Christian Anfmsen s experiments demonstrated that proteins can fold reversibly. A corollary result of Anfmsen s work is that the native structures of at least some globular proteins are thermodynamically stable states. But the matter of how a given protein achieves such a stable state is a complex one. Cyrus Levinthal pointed out in 1968 that so many conformations are possible for a typical protein that the protein does not have sufficient time to reach its most stable conformational state by sampling all the possible conformations. This argument, termed Levinthal s paradox, goes as follows consider a protein of 100 amino acids. Assume that there are only two conformational possibilities per amino acid, or = 1.27 X 10 ° possibilities. Allow 10 sec for... 

Irback A, Sjunnesson F. Folding thermodynamics of three beta-sheet peptides a model study. Proteins 2004 56 110-6. 

We present a molecular theory of hydration that now makes possible a unification of these diverse views of the role of water in protein stabilization. The central element in our development is the potential distribution theorem. We discuss both its physical basis and statistical thermodynamic framework with applications to protein solution thermodynamics and protein folding in mind. To this end, we also derive an extension of the potential distribution theorem, the quasi-chemical theory, and propose its implementation to the hydration of folded and unfolded proteins. Our perspective and current optimism are justified by the understanding we have gained from successful applications of the potential distribution theorem to the hydration of simple solutes. A few examples are given to illustrate this point. 

Ensemble for Protein Folding Ground State Search and Thermodynamics. 

Livingstone, J.R., R.S. Spolar, and M.T. Record, Jr. 1991. Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry 30 4237 1244. 

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