Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins.

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.

journal_name

Protein Pept Lett

authors

Arakawa T,Tokunaga M

doi

10.2174/0929866043478220

subject

Has Abstract

pub_date

2004-04-01 00:00:00

pages

125-32

issue

2

eissn

0929-8665

issn

1875-5305

journal_volume

11

pub_type

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