An osmolyte effect on the heat capacity change for protein folding

Biochemistry
I M Plaza del Pino, J M Sanchez-Ruiz

Abstract

We have carried out a differential scanning calorimetry study into the pH effect on the thermal denaturation of ribonuclease A at several concentrations of the osmolyte sarcosine. In order to properly analyze these data, we have elaborated the thermodynamic theory of the linkage between temperature, cosolvent, and pH effects. The denaturation heat capacity increases with sarcosine concentration. The effects of temperature and sarcosine concentration on the denaturation enthalpy and entropy values are well described by convergence equations, with convergence temperatures of around 100 degrees C for the enthalpy and around 112 degrees C for the entropy; we suggest that these effects might be related to a solvent-induced alteration of the apolar-group-hydration contribution to the folding thermodynamics. From our data, we estimate that about 70 extra molecules of water are thermodynamically bound upon ribonuclease denaturation in diluted aqueous solutions of sarcosine; this number is 6-9 times smaller than that predicted on the basis of the following two premises: (a) the osmolyte is strongly excluded from the surface of both the native and the denatured protein and (b) the denatured state is a fully solvated chain. We suggest tha...Continue Reading

Citations

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