Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins |
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Authors: | Arakawa Tsutomu Tokunaga Masao |
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Institution: | Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, USA. Tarakawa@aol.com |
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Abstract: | In general, halophilic proteins are stable only in the presence of salts at high concentrations. Not only is high salt concentration important for structural stability of halophilic proteins, but also refolding of a denatured halophilic protein requires high salt concentration. This review summarizes the importance of electrostatic charge shielding and hydrophobic interactions in the stability and refolding of halophilic proteins. |
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