title: Slow unfolding of monomeric proteins from hyperthermophiles with reversible unfolding.
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.
authors.affiliation: Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan.
authors.forename: Atsushi
authors.initials: A
authors.lastname: Mukaiyama
authors.affiliation: Department of Material and Life Science, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.|CREST, JST, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
authors.forename: Kazufumi
authors.initials: K
authors.lastname: Takano
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D011489:Protein Denaturation; D017510:Protein Folding; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D016914:Ribonuclease H / Q000737:chemistry / Q000378:metabolism; D019712:Thermococcus / Q000201:enzymology; D013816:Thermodynamics
chemical_list: D011506:Proteins; C091139:ribonuclease HII; D016914:Ribonuclease H