The hydrophobic effect and its role in cold denaturation

C.L. Dias, T. Ala-Nissila, J. Wong-ekkabut, I. Vattulainen, M. Grant, M.E.J. Karttunen

    Research output: Contribution to journalArticleAcademicpeer-review

    101 Citations (Scopus)

    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. Keywords: Hydrophobic effect; Thermodynamics; Clathrate cages; Hydrate cages; Cold denaturation; Proteins
    Original languageEnglish
    Pages (from-to)91-99
    JournalCryobiology
    Volume60
    Issue number1
    DOIs
    Publication statusPublished - 2010

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