Sturtevant J M
Proc Natl Acad Sci U S A. 1977 Jun;74(6):2236-40. doi: 10.1073/pnas.74.6.2236.
Six possible sources of the large heat capacity and entropy changes frequently observed for processes involving proteins are identified. Of these the conformational, hydrophobic, and vibrational effects seem likely to be of greatest importance. A method is proposed for estimating the magnitudes of the hydrophobic and vibrational contributions. Application of this method to several protein processes appears to achieve significant clarification of previously confusing and apparently contradictory data.
确定了在涉及蛋白质的过程中经常观察到的大比热容和熵变的六种可能来源。其中,构象、疏水和振动效应似乎最为重要。提出了一种估算疏水和振动贡献大小的方法。将该方法应用于几个蛋白质过程似乎能显著澄清以前令人困惑且明显矛盾的数据。