Ragone R, Colonna G
Department of Biochemistry and Biophysics, II University of Naples, Italy.
J Biol Chem. 1994 Feb 11;269(6):4047-9.
We find that isoenthalpic and isoentropic temperatures characterizing the unfolding of small globular proteins are linked by a simple relationship, which takes into account the occurrence of common values of specific unfolding enthalpy and entropy changes. The difference between these temperatures implies that the hydration effect favors protein folding over a quite large range of temperatures.
我们发现，表征小分子球状蛋白质去折叠过程的等焓温度和等熵温度通过一种简单关系相联系，该关系考虑了特定去折叠焓和熵变的共同值的出现。这些温度之间的差异意味着，在相当大的温度范围内，水合作用有利于蛋白质折叠。
