Electrochemistry
Online ISSN : 2186-2451
Print ISSN : 1344-3542
ISSN-L : 1344-3542
Communications
Conformational Stability of a Hyperthermophilic Protein in Various Conditions for Denaturation
Kentaro SHIRAKIShinsuke FUJIWARATadayuki IMANAKAMasahiro TAKAGI
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JOURNALS OPEN ACCESS

2001 Volume 69 Issue 12 Pages 949-952

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Abstract

Although hyperthermophilic proteins retain their native forms even under high temperature environments, it is not well characterized whether they show some tolerance toward other denaturing conditions. In this study, we examined tolerance of a hyperthermophilic protein to various denaturing conditions using O6-methylguanine-DNA methyltransferase from Thermococcus kodakaraensis KOD1 (Tk-MGMT) as a model protein. Tk-MGMT showed higher stability to alcohols and denaturants as well as higher melting temperature than its mesophilic counterpart protein from Escherichia coli (Ec-AdaC). High stability toward various denaturing conditions suggests that hyperthermophilic proteins can be commercially applied to use in various extreme conditions as well as high temperature environments.

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© 2001 The Electrochemical Society of Japan
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