Slow unfolding of monomeric proteins from hyperthermophiles with reversible unfolding

Int J Mol Sci. 2009 Mar;10(3):1369-85. doi: 10.3390/ijms10031369. Epub 2009 Mar 24.

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; equilibrium and kinetic; folding/unfolding; stability.

Publication types

  • Review

MeSH terms

  • Hydrophobic and Hydrophilic Interactions
  • Kinetics
  • Protein Denaturation
  • Protein Folding
  • Protein Stability
  • Proteins / chemistry*
  • Proteins / metabolism
  • Ribonuclease H / chemistry
  • Ribonuclease H / metabolism
  • Thermococcus / enzymology
  • Thermodynamics

Substances

  • Proteins
  • ribonuclease HII
  • Ribonuclease H