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Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability.

Hennig, Michael and Sterner, Reinhard and Kirschner, Kasper and Jansonius, J. N. (1997) Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability. Biochemistry 36 (20), pp. 6009-16.

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Abstract

The structural basis of thermostability of proteins is of great scientific and biotechnological interest. Differences in the X-ray structues of orthologous proteins from hyperthermophilic and mesophilic organisms can indicate crucial stabilizing interactions. To this end the crystal structure of dimeric phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima (tPRAI) ...

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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
9166771PubMed ID
10.1021/bi962718qDOI
Classification:
NotationType
Aldose-Ketose IsomerasesMESH
Amino Acid SequenceMESH
Binding SitesMESH
Carbohydrate Epimerases/chemistryMESH
Computer SimulationMESH
Crystallography, X-RayMESH
DimerizationMESH
Enzyme StabilityMESH
Escherichia coli/enzymologyMESH
Gram-Negative Anaerobic Bacteria/enzymologyMESH
Hot TemperatureMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Protein Structure, SecondaryMESH
Protein Structure, TertiaryMESH
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 09:18
Last Modified:22 Mar 2010 09:51
Item ID:13708
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