Microscopic Mechanism for Cold Denaturation
Loading...
Access rights
© 2008 American Physical Society (APS). http://www.aps.org/
URL
Journal Title
Journal ISSN
Volume Title
School of Science |
A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
Unless otherwise stated, all rights belong to the author. You may download, display and print this publication for Your own personal use. Commercial use is prohibited.
Date
2008
Major/Subject
Mcode
Degree programme
Language
en
Pages
118101/1-4
Series
Physical Review Letters, Volume 100, Issue 11
Abstract
We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in favor of solvent-separated configurations, the same mechanism seen in pressure-induced denaturation. A phenomenological explanation proposed for the mechanism is suggested as being responsible for cold denaturation in real proteins.Description
Keywords
proteins, protein unfolding, denaturation
Other note
Citation
Dias, Cristiano L. & Ala-Nissilä, Tapio & Karttunen, Mikko & Vattulainen, Ilpo & Grant, Martin. 2008. Microscopic Mechanism for Cold Denaturation. Physical Review Letters. Volume 100, Issue 11. P. 118101/1-4. ISSN 0031-9007 (printed). DOI: 10.1103/physrevlett.100.118101.