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Int. J. Mol. Sci. 2009, 10(3), 1369-1385; doi:10.3390/ijms10031369

Slow Unfolding of Monomeric Proteins from Hyperthermophiles with Reversible Unfolding

1
Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan
2
Department of Material and Life Science, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan
3
CREST, JST, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan
*
Author to whom correspondence should be addressed.
Received: 28 January 2009 / Revised: 19 March 2009 / Accepted: 23 March 2009 / Published: 24 March 2009
(This article belongs to the Special Issue Protein Folding 2009)
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Abstract

Based on the differences in their optimal growth temperatures microorganisms can be classified into psychrophiles, mesophiles, thermophiles, and hyperthermophiles. Proteins from hyperthermophiles generally exhibit greater stability than those from other organisms. In this review, we collect data about the stability and folding of monomeric proteins from hyperthermophilies with reversible unfolding, from the equilibrium and kinetic aspects. The results indicate that slow unfolding is a general strategy by which proteins from hyperthermophiles adapt to higher temperatures. Hydrophobic interaction is one of the factors in the molecular mechanism of the slow unfolding of proteins from hyperthermophiles. View Full-Text
Keywords: Proteins from hyperthermophiles; folding/unfolding; stability; equilibrium and kinetic Proteins from hyperthermophiles; folding/unfolding; stability; equilibrium and kinetic
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Mukaiyama, A.; Takano, K. Slow Unfolding of Monomeric Proteins from Hyperthermophiles with Reversible Unfolding. Int. J. Mol. Sci. 2009, 10, 1369-1385.

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