The stability of proteins in extreme environments

Jaenicke, Rainer and Böhm, Gerald (1998) The stability of proteins in extreme environments. CURRENT OPINION IN STRUCTURAL BIOLOGY, 8 (6). pp. 738-748. ISSN 0959-440X, 1879-033X

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Abstract

Three complete genome sequences of thermophilic bacteria provide a wealth of information challenging current ideas concerning phylogeny and evolution, as well as the determinants of protein stability Considering known protein structures from extremophiles, it becomes clear that no general conclusions can be drawn regarding adaptive mechanisms to extremes of physical conditions. Proteins are individuals that accumulate increments of stabilization; in thermophiles these come from charge clusters, networks of hydrogen bonds, optimization of packing and hydrophobic interactions, each in its own way. Recent examples indicate ways for the rational design of ultrastable proteins.

Item Type: Article
Uncontrolled Keywords: BACTERIUM THERMOTOGA-MARITIMA; PHOSPHORIBOSYL ANTHRANILATE ISOMERASE; ARCHAEON PYROCOCCUS-FURIOSUS; SITE-DIRECTED MUTAGENESIS; TIM FUSION PROTEIN; CRYSTAL-STRUCTURE; TRIOSEPHOSPHATE ISOMERASE; PHOSPHOGLYCERATE KINASE; 3-ISOPROPYLMALATE DEHYDROGENASE; HYPERTHERMOPHILIC ARCHAEA
Subjects: 500 Science > 570 Life sciences
Divisions: Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie
Depositing User: Dr. Gernot Deinzer
Date Deposited: 09 Feb 2023 07:37
Last Modified: 09 Feb 2023 07:37
URI: https://pred.uni-regensburg.de/id/eprint/49278

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