Thermodynamics of protein folding

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. 

Lee and Richards (1971) defined the solvent-accessible surface as that described by the center of a solvent molecule rolled about the surface of a solute molecule. This concept and its offspring are the basis of various computations of the contribution of hydration to the thermodynamics of protein folding and the thermodynamics of protein interactions. Ed-sall and McKenzie (1983) reviewed the literature on the thermodynamics of transfer processes used to model hydration and correlated this information with protein structure results analyzed according to the Lee and Richards formalism. Other notable reviews are those by Richards (1977), Nemethy et al. (1981), and Nemethy (1986). 

See also a-Helix, / -Sheet, Factors Determining Secondary and Tertiary Structure, Thermodynamics of Protein Folding, Dynamics of Protein Folding, Covalent Modifications to Regulate Enzyme Activity (from Chapter 11). 

See also Thermodynamics of Protein Folding, Dynamics of Protein Folding,... 

E. I. Shakhnovich and A. M. Gutin, Implications of the Thermodynamics of Protein Folding form Evolution of Primary Sequences, Nature 346,773-775 (1990). 

M.-H. Hao and H. A. Scheraga, /. Chem. Phys., 102, 1334 (1995). Statistical Thermodynamics of Protein Folding Comparison of Mean Field Theory with Monte Carlo Simulation. 

Hydration for the Kinetics and Thermodynamics of Protein Folding Simplified Lattice Models. 

Some of the vacuum theories treated earlier in the book are repeated in Chapter 8. Examples are chemical equilibrium, allosteric phenomena, and helix-coil transition. The general procedure to transform a vacuum theory into a solution theory is developed. Then we emphasize possible large solvent effects that can significantly alter the vacuum theory, especially when the solvent is water. A detailed account of the thermodynamics of protein folding and protein association is also presented. 

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