CaltechAUTHORS
  A Caltech Library Service

Some Thermodynamic Implications for the Thermostability of Proteins

Rees, Douglas C. and Robertson, Andrew D. (2001) Some Thermodynamic Implications for the Thermostability of Proteins. Protein Science, 10 (6). pp. 1187-1194. ISSN 0961-8368. PMCID PMC2374017. https://resolver.caltech.edu/CaltechAUTHORS:20150108-153227470

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20150108-153227470

Abstract

An analysis of the thermodynamics of protein stability reveals a general tendency for proteins that denature at higher temperatures to have greater free energies of maximal stability. To a reasonable approximation, the temperature of maximal stability for the set of globular, water-soluble proteins surveyed by Robertson and Murphy occurs at T* ∼283K, independent of the heat denaturation temperature, T_m. This observation indicates, at least for these proteins, that thermostability tends to be achieved through elevation of the stability curve rather than by broadening or through a horizontal shift to higher temperatures. The relationship between the free energy of maximal stability and the temperature of heat denaturation is such that an increase in maximal stability of ∼0.008 kJ/mole/residue is, on average, associated with a 1°C increase in T_m. An estimate of the energetic consequences of thermal expansion suggests that these effects may contribute significantly to the destabilization of the native state of proteins with increasing temperature.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1110/ps.180101DOIArticle
http://onlinelibrary.wiley.com/doi/10.1110/ps.180101/abstractPublisherArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2374017/PubMed CentralArticle
ORCID:
AuthorORCID
Rees, Douglas C.0000-0003-4073-1185
Contact Email Address:phoebe@caltech.edu
Additional Information:© 2001 The Protein Society. Received January 16, 2001; Final Revision March 15, 2001; Accepted March 15, 2001. This work was supported in part by National Institutes of General Medical Sciences grants GM45162 to D.C.R. and GM46869 to A.D.R. The publication costs of this article were defrayed in part by payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 USC section 1734 solely to indicate this fact.
Funders:
Funding AgencyGrant Number
National Institutes of General Medical SciencesGM45162
National Institutes of General Medical SciencesGM46869
Subject Keywords:Protein stability; thermal expansion; protein volumes; stability curve
Issue or Number:6
PubMed Central ID:PMC2374017
Record Number:CaltechAUTHORS:20150108-153227470
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150108-153227470
Official Citation:Rees, D. C. and Robertson, A. D. (2001), Some thermodynamic implications for the thermostability of proteins. Protein Science, 10: 1187–1194. doi: 10.1110/ps.180101
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53401
Collection:CaltechAUTHORS
Deposited By: SWORD User
Deposited On:13 Jan 2015 20:15
Last Modified:03 Oct 2019 07:49

Repository Staff Only: item control page