Stability of cellular proteins under supraphysiological temperatures

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

Stability of cellular proteins under supraphysiological temperatures

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

Research output: Chapter in Book/Report/Conference proceeding › Conference 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 language	English (US)
Title of host publication	Annual International Conference of the IEEE Engineering in Medicine and Biology - Proceedings
Pages	5440-5443
Number of pages	4
Volume	26 VII
State	Published - 2004
Externally published	Yes
Event	Conference Proceedings - 26th Annual International Conference of the IEEE Engineering in Medicine and Biology Society, EMBC 2004 - San Francisco, CA, United States Duration: Sep 1 2004 → Sep 5 2004

Other

Other	Conference Proceedings - 26th Annual International Conference of the IEEE Engineering in Medicine and Biology Society, EMBC 2004
Country	United States
City	San Francisco, CA
Period	9/1/04 → 9/5/04

ASJC Scopus subject areas

Bioengineering

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Despa, F, Orgill, DP & Lee, RC 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, Conference Proceedings - 26th Annual International Conference of the IEEE Engineering in Medicine and Biology Society, EMBC 2004, San Francisco, CA, United States, 9/1/04.

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language = "English (US)",

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AU - Despa, F.

AU - Orgill, D. P.

AU - Lee, R. C.

PY - 2004

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N2 - 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.

AB - 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.

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AN - SCOPUS:11144322217

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BT - Annual International Conference of the IEEE Engineering in Medicine and Biology - Proceedings

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Y2 - 1 September 2004 through 5 September 2004

ER -

Stability of cellular proteins under supraphysiological temperatures

Abstract

Other

ASJC Scopus subject areas

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