The hydrophobic effect and its role in cold denaturation.
The hydrophobic effect is considered the main driving force for protein folding and plays an important role in the stability of those biomolecules. Cold denaturation, where the native state of the protein loses its stability upon cooling, is also attributed to this effect. It is therefore not surprising that a lot of effort has been spent in understanding this phenomenon. Despite these efforts, many unresolved fundamental aspects remain. In this paper we review and summarize the thermodynamics of proteins, the hydrophobic effect and cold denaturation. We start by accounting for these phenomena macroscopically then move to their atomic-level description. We hope this review will help the reader gain insights into the role played by the hydrophobic effect in cold denaturation.
Dias
Cristiano L
CL
Department of Applied Mathematics, The University of Western Ontario, Middlesex College, 1151 Richmond St. N., London, Ont., Canada N6A 5B7. diasc@physics.mcgill.ca
Ala-Nissila
Tapio
T
Wong-ekkabut
Jirasak
J
Vattulainen
Ilpo
I
Grant
Martin
M
Karttunen
Mikko
M
D000818:Animals; D001703:Biophysics / Q000379:methods; D003080:Cold Temperature; D015925:Cryopreservation / Q000379:methods*; D003451:Cryoprotective Agents / Q000494:pharmacology; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D015233:Models, Statistical; D008968:Molecular Conformation; D011108:Polymers / Q000737:chemistry; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry; D013816:Thermodynamics
D003451:Cryoprotective Agents; D011108:Polymers; D011506:Proteins