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Updated: Aug 24, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins
Tsutomu Arakawa1, Masao Tokunaga
1Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, USA. Tarakawa@aol.com
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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