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:

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:

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

DOI https://dx.doi.org/10.2174/0929866043478220	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305