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Thermophilic adaptation of proteins.

Sterner, Reinhard and Liebl, W. (2001) Thermophilic adaptation of proteins. Critical reviews in biochemistry and molecular biology 36 (1), pp. 39-106.

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Abstract

Hyperthermophilic organisms optimally grow close to the boiling point of water. As a consequence, their macromolecules must be much more thermostable than those from mesophilic species. Here, proteins from hyperthermophiles and mesophiles are compared with respect to their thermodynamic and kinetic stabilities. The known differences in amino acid sequences and three-dimensional structures between ...

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Item type:Article
Date:2001
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
11256505PubMed ID
10.1080/20014091074174DOI
Classification:
NotationType
Adaptation, BiologicalMESH
Amino Acid SequenceMESH
Archaea/metabolismMESH
Bacteria/metabolismMESH
Directed Molecular EvolutionMESH
EnvironmentMESH
Enzyme StabilityMESH
Heat-Shock Proteins/metabolismMESH
Hot TemperatureMESH
Molecular Chaperones/metabolismMESH
Mutagenesis, Site-Directed/geneticsMESH
Protein FoldingMESH
Protein Structure, TertiaryMESH
Proteins/metabolismMESH
Species SpecificityMESH
Static ElectricityMESH
ThermodynamicsMESH
Thermus/metabolismMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:13700
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