The hydrophobic effect and its role in cold denaturation

Cristiano L. Dias, Tapio Ala-Nissila, Jirasak Wong-ekkabut, Ilpo Vattulainen, Martin Grant, Mikko Karttunen

Research output: Contribution to journalReview articlepeer-review

105 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)91-99
Number of pages9
JournalCryobiology
Volume60
Issue number1
DOIs
StatePublished - Feb 2010
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

Keywords

  • Clathrate cages
  • Cold denaturation
  • Hydrate cages
  • Hydrophobic effect
  • Proteins
  • Thermodynamics

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