Protein folding/unfolding transition

VJ Hilser, CD Worosila, E Freire. Analysis of thermal-induced proteins folding/ unfolding transitions using free-solution capillary electrophoresis. Anal. Biochem. 208 125-131 (1993). 

Freire E. Statistical thermodynamic analysis of (he heat capacity function associated with protein folding-unfolding transitions. Coimnents Mol Cell Biophys 1989 6(2) 123-140. 

An interesting aspect of the photoreaction of PYP is the similarity to the protein folding/unfolding reaction. Hellingwerf and his coworkers applied the transition state theory to the photoreaction of PYP and estimated the thermodynamic parameters, the entropy, enthalpy, and heat capacity changes of activation [29]. They also carried out thermodynamic analysis on the thermal denaturation of PYP. Consequently, they found that the heat capacity changes in the photoreaction are comparable to those in the unfolding... 

R. Day and V. Daggett, Protein Sci., 14, 1242 (2005). Sensitivity of the Folding/Unfolding Transition State Ensemble of Chymotrypsin Inhibitor 2 to Changes in Temperature and Solvent. 

Thermodynamic parameters can be defined only for a reversible process. The midpoint corresponding to a thermally reversible folding-unfolding transition of a protein is defined by the temperature of transition, (i.e., the temperature at which the apparent transition constant K is equal to 1, and AG, the variation of free energy, is nul under conditions where a two-state approximation is valuable). Under these conditions is equal to AH/AS and AG is equal to AH(1 — T/T ). The different parameters are defined in Chapter 6 however, it is noted here that Privalov and Khechinaschvili (1974) have shown that AH is a linear function of temperature for a number... 

Protein surface Bound water relaxation Side chain rotational correlation Proton transfer reaction of ionizable side chains Protein conformation Local motion Isomerization process Folding-unfolding transition Enzyme substrate complex in solution Encounter rate... 

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