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

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

VOLUME: 11 ISSUE: 2

Author(s):Tsutomu Arakawa and Masao Tokunaga

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

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

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.

Cite this article as:

Tsutomu Arakawa and Masao Tokunaga, “ Electrostatic and Hydrophobic Interactions Play A Major Role in the Stability and Refolding of Halophilic Proteins.”, Protein & Peptide Letters (2004) 11: 125. https://doi.org/10.2174/0929866043478220

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