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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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)