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Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima.

Macedo-Ribeiro, S. and Darimont, Beatrice and Sterner, Reinhard and Huber, R. (1996) Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima. Structure (London, England : 1993) 4 (11), pp. 1291-301.

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Abstract

BACKGROUND: The characterization of the structural features that account for the high thermostability of some proteins is of great scientific and biotechnological interest. Proteins from hyperthermophilic organisms with optimum growth temperatures of 80 degrees C and higher generally show high intrinsic stabilities. The comparison of high resolution X-ray structures of these proteins with their ...

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Item Type:Article
Date:1996
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
8939753PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
Bacterial Proteins/chemistryMESH
Computer SimulationMESH
Crystallography, X-RayMESH
Ferredoxins/classificationMESH
Gram-Negative Anaerobic Bacteria/chemistryMESH
Hot TemperatureMESH
Hydrogen BondingMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Protein ConformationMESH
Protein DenaturationMESH
Sequence Homology, Amino AcidMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner: Universitätsbibliothek Regensburg
Deposited On:22 Mar 2010 09:23
Last Modified:22 Mar 2010 09:24
Item ID:13710
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