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Electrostatic and Hydrophobic Interactions Play A Major Role in the Stability and Refolding of Halophilic Proteins.

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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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Keywords: halophilic; nucleoside diphosphate kinase; refolding; salt

Document Type: Review Article

Affiliations: Alliance Protein Laboratories, 3957 Corte Cancion, Thousand Oaks, CA 91360, U.S.A.

Publication date: 2004-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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