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 |
Fingerprint
ASJC Scopus subject areas
- Bioengineering
Cite this
Stability of cellular proteins under supraphysiological temperatures. / Despa, F.; Orgill, D. P.; Lee, R. C.
Annual International Conference of the IEEE Engineering in Medicine and Biology - Proceedings. Vol. 26 VII 2004. p. 5440-5443.Research output: Chapter in Book/Report/Conference proceeding › Conference contribution
}
TY - GEN
T1 - Stability of cellular proteins under supraphysiological temperatures
AU - Despa, F.
AU - Orgill, D. P.
AU - Lee, R. C.
PY - 2004
Y1 - 2004
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.
UR - http://www.scopus.com/inward/record.url?scp=11144322217&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=11144322217&partnerID=8YFLogxK
M3 - Conference contribution
VL - 26 VII
SP - 5440
EP - 5443
BT - Annual International Conference of the IEEE Engineering in Medicine and Biology - Proceedings
ER -