Arnvig, KB;
Pedersen, S;
Sneppen, K;
(2000)
Thermodynamics of heat-shock response.
Physical Review Letters
, 84
(13)
pp. 3005-3008.
10.1103/PhysRevLett.84.3005.
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Abstract
Production of heat-shock proteins is induced when a living cell is exposed to a rise in temperature. The heat-shock response of protein DnaK synthesis in E.coli for temperature shifts T → T + ΔT and T → T - ΔT is measured as a function of the initial temperature T. We observe a reversed heat shock at low T. The magnitude of the shock increases when one increases the distance to the temperature T ≈ 23 °C, thereby mimicking the nonmonotonous stability of proteins at low temperature. This suggests that stability related to hot as well as cold unfolding of proteins is directly implemented in the biological control of protein folding. © 2000 The American Physical Society.
| Type: | Article |
|---|---|
| Title: | Thermodynamics of heat-shock response |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1103/PhysRevLett.84.3005 |
| Publisher version: | http://dx.doi.org/10.1103/PhysRevLett.84.3005 |
| Language: | English |
| Additional information: | © 2000 The American Physical Society |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology |
| URI: | https://discovery.ucl.ac.uk/id/eprint/1393270 |
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