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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

Author(s): Tsutomu Arakawa and Masao Tokunaga

Volume 11, Issue 2, 2004

Page: [125 - 132] Pages: 8

DOI: 10.2174/0929866043478220

Price: $65


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.

Keywords: halophilic,, salt,, nucleoside diphosphate kinase,, refolding,

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