Stability of cellular proteins under supraphysiological temperatures

F. Despa, D. P. Orgill, R. C. Lee

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

We present quantitative analyses of the kinetics of cellular components confronted with the destabilizing effect of irreversible thermal denaturation. We examine the dependence of the thermal denaturation on the heating rate, relative stability, population and lifetime of the states involved in transition and crowding effects. We propose a mechanism for self-stabilization of proteins during unfolding in tightly packed fibers and membranes. Speaking in terms of vulnerability to thermal denaturation, our results suggest that the thermal alteration of the plasma membrane is likely to be the most significant cause of the tissue necrosis.

Original languageEnglish (US)
Title of host publicationAnnual International Conference of the IEEE Engineering in Medicine and Biology - Proceedings
Pages5440-5443
Number of pages4
Volume26 VII
StatePublished - 2004
Externally publishedYes
EventConference Proceedings - 26th Annual International Conference of the IEEE Engineering in Medicine and Biology Society, EMBC 2004 - San Francisco, CA, United States
Duration: Sep 1 2004Sep 5 2004

Other

OtherConference Proceedings - 26th Annual International Conference of the IEEE Engineering in Medicine and Biology Society, EMBC 2004
CountryUnited States
CitySan Francisco, CA
Period9/1/049/5/04

ASJC Scopus subject areas

  • Bioengineering

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  • Cite this

    Despa, F., Orgill, D. P., & Lee, R. C. (2004). Stability of cellular proteins under supraphysiological temperatures. In Annual International Conference of the IEEE Engineering in Medicine and Biology - Proceedings (Vol. 26 VII, pp. 5440-5443)