Protein heat capacity: inconsistencies in the current view of cold denaturation

被引:23
作者
Hallerbach, B [1 ]
Hinz, HJ [1 ]
机构
[1] Univ Munster, Inst Phys Chem, D-48143 Munster, Germany
关键词
DSC; cold denaturation; hydration entropy; second law; independent and coupled processes; fluctuations; enthalpy partitioning;
D O I
10.1016/S0301-4622(98)00239-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The present study shows on the basis of the thermodynamic stability criterion (partial derivative S/partial derivative T)(p) > 0 that partitioning of the entropy of cold-unfolding of a protein into independent positive conformational and negative hydrational contributions is incorrect. Furthermore it provides a new microscopic interpretation of protein heat capacity that takes into account the significant fluctuations in energy and entropy which result from the small size of these macromolecules. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:219 / 227
页数:9
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