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

Tsutomu      Arakawa; Masao      Tokunaga

doi:10.2174/0929866043478220

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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Protein & Peptide Letters

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

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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.

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Arakawa Tsutomu and Tokunaga Masao, Electrostatic and Hydrophobic Interactions Play A Major Role in the Stability and Refolding of Halophilic Proteins., Protein & Peptide Letters 2004; 11 (2) . https://dx.doi.org/10.2174/0929866043478220