Theory of cold denaturation of proteins

Arieh Ben-Naim

Department of Physical Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Jerusalem.

DOI: 10.4236/abc.2013.31005                

Abstract

A new approach to the problem of cold denaturation is presented. It is based on solvent-induced effects operating on hydrophilic groups along the protein. These effects are stronger than the corresponding hydrophobic effects, and they operate on the hydrophilic groups which are plentiful than hydrophobic groups. It is shown that both heat and cold denaturation can be explained by these hydrophilic effects.

Keywords

Protein Folding; Cold Denaturation; Hydrophobic; Hydrophilic Effects

Conflicts of Interest

The authors declare no conflicts of interest.

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