Title: Electrostatic and Hydrophobic Interactions Play A Major Role in the Stability and Refolding of Halophilic Proteins.
VOLUME: 11 ISSUE: 2
Author(s):Tsutomu Arakawa and Masao Tokunaga
Affiliation:Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, U.S.A.
Keywords:halophilic,, salt,, nucleoside diphosphate kinase,, refolding,
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.