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

Author(s): Tsutomu Arakawa, Masao Tokunaga.

Journal Name: Protein & Peptide Letters

Volume 11 , Issue 2 , 2004

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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.

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

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Article Details

VOLUME: 11
ISSUE: 2
Year: 2004
Page: [125 - 132]
Pages: 8
DOI: 10.2174/0929866043478220
Price: $58

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