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

Slow Unfolding of Monomeric Proteins from Hyperthermophiles with Reversible Unfolding

1
 and 2, 3,*
Received: 28 January 2009; in revised form: 19 March 2009 / Accepted: 23 March 2009 / Published: 24 March 2009
(This article belongs to the Special Issue Protein Folding)
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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.
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 which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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.

AMA Style

Mukaiyama A, Takano K. Slow Unfolding of Monomeric Proteins from Hyperthermophiles with Reversible Unfolding. International Journal of Molecular Sciences. 2009; 10(3):1369-1385.

Chicago/Turabian Style

Mukaiyama, Atsushi; Takano, Kazufumi. 2009. "Slow Unfolding of Monomeric Proteins from Hyperthermophiles with Reversible Unfolding." Int. J. Mol. Sci. 10, no. 3: 1369-1385.



Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert