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Pace N.C. and Tanford C. (1968) Thermodynamics of the unfolding of beta-lactoglobulin A in aqueous urea solutions between 5 and 55 degrees. Biochemistry, 7, 198 208. doi:10.1021/bi00841a025

has been cited by the following article:

• TITLE: Theory of cold denaturation of proteins

  AUTHORS: Arieh Ben-Naim

  KEYWORDS: Protein Folding; Cold Denaturation; Hydrophobic; Hydrophilic Effects

  JOURNAL NAME: Advances in Biological Chemistry, Vol.3 No.1, February 17, 2013

  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.