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Structural features correlated with the extreme thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima.

Macedo-Ribeiro, S. and Darimont, Beatrice and Sterner, Reinhard (1997) Structural features correlated with the extreme thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima. Biological chemistry 378 (3-4), pp. 331-6.

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Abstract

Understanding the molecular mechanisms behind extreme temperature stability is of relevance for the protein folding problem and for designing proteins for industrial and medical applications. A powerful approach for understanding the structural basis of thermostability is the comparison of high resolution structures of homologous proteins from mesophiles and thermophiles. The 1.75 A crystal ...

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Item Type:Article
Date:1997
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
9165090PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
Crystallography, X-RayMESH
Ferredoxins/chemistryMESH
Gram-Negative Anaerobic Bacteria/chemistryMESH
Hot TemperatureMESH
Hydrogen BondingMESH
Iron/chemistryMESH
Molecular Sequence DataMESH
Protein ConformationMESH
Sulfur/chemistryMESH
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 09:20
Last Modified:22 Mar 2010 09:51
Item ID:13709
Owner Only: item control page
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