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

by: B Hallerbach, Hinz

Biophysical Chemistry, Vol. 76, No. 3. (22 February 1999), pp. 219-227.

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Abstract

The present study shows on the basis of the thermodynamic stability criterion ([partial differential]S/[partial differential]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.

@article{citeulike:2208638, abstract = {The present study shows on the basis of the thermodynamic stability criterion ([partial differential]S/[partial differential]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.}, author = {Hallerbach, B. and Hinz}, citeulike-article-id = {2208638}, doi = {http://dx.doi.org/10.1016/S0301-4622(98)00239-7}, journal = {Biophysical Chemistry}, keywords = {cold-denaturation, hydrophobicity, secondary-structures, thermodynamics}, month = {February}, number = {3}, pages = {219--227}, posted-at = {2008-01-08 19:47:31}, priority = {5}, title = {Protein heat capacity: inconsistencies in the current view of cold denaturation}, url = {http://dx.doi.org/10.1016/S0301-4622(98)00239-7}, volume = {76}, year = {1999} }

RIS record

TY - JOUR ID - citeulike:2208638 L3 - citeulike-article-id:2208638 TI - Protein heat capacity: inconsistencies in the current view of cold denaturation JF - Biophysical Chemistry VL - 76 IS - 3 SP - 219 EP - 227 N2 - The present study shows on the basis of the thermodynamic stability criterion ([partial differential]S/[partial differential]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. KW - cold-denaturation KW - hydrophobicity KW - secondary-structures KW - thermodynamics AU - Hallerbach, B AU - Hinz PY - 1999/02/22/ UR - http://dx.doi.org/10.1016/S0301-4622(98)00239-7 ER -

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