title: Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins.
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.
authors.affiliation: Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, USA. Tarakawa@aol.com
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Arakawa
authors.forename: Masao
authors.initials: M
authors.lastname: Tokunaga
mesh_terms: D004795:Enzyme Stability; D019617:Halobacterium salinarum / Q000737:chemistry / Q000201:enzymology*; D057927:Hydrophobic and Hydrophilic Interactions; D009701:Nucleoside-Diphosphate Kinase / Q000737:chemistry*; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012492:Salts / Q000737:chemistry*; D055672:Static Electricity; D013816:Thermodynamics
chemical_list: D012492:Salts; D009701:Nucleoside-Diphosphate Kinase