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

Become EABM
Become Reviewer


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,

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2004
Page: [125 - 132]
Pages: 8
DOI: 10.2174/0929866043478220
Price: $65

Article Metrics

PDF: 8