Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins.
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.
Arakawa
Tsutomu
T
Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, USA. Tarakawa@aol.com
Tokunaga
Masao
M
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
D012492:Salts; D009701:Nucleoside-Diphosphate Kinase