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[ccp4bb]: Thermostability vs Structure
Hi,
You should have a look at this article
Trends in Biochemical Sciences
Full A-Z Journal ListIssues ListVol. 26, No. 9, September 2001 Abstract
Ion pairs and the thermotolerance of proteins from hyperthermophiles: a 'traffic rule' for hot roads [Review]
Andrey Karshikoff and Rudolf Ladenstein
Trends in Biochemical Sciences, 2001, 26:9:550-556
Abstract
The proteins from hyperthermophilic organisms maintain their biologically active structure at temperatures that
are significantly higher than the denaturation temperatures of their mesophilic counterparts. The fact that there is
usually a high degree of sequence and structural homology between these two classes of proteins suggests that
the source of this extreme thermal tolerance is hidden in the delicate balance of the non-covalent interactions.
Among the large number of factors identified in the literature as being responsible for the thermostability of these
proteins, this article focuses on electrostatic interactions. It demonstrates that the optimization of electrostatic
interactions by increasing of the number of salt bridges is a driving force for enhancement of the
thermotolerance of proteins from hyperthermophilic microorganisms. This feature is less evident in proteins from
thermophilic organisms and is absent from mesophile-derived proteins.
Regards,
Greg
________________________________________________________________
Gregory Verdon
Laboratory of Biophysical Chemistry
Department of Chemistry
University of Groningen
Nijenborgh 4 tel : +31(50)3634384
9747 AG Groningen fax : +31(50)3634800
The Netherlands e-mail: g.verdon@chem.rug.nl
________________________________________________________________