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1H nuclear-magnetic-resonance investigation of oxidized Fe4S4 ferredoxin from Thermotoga maritima. Hyperfine-shifted resonances, sequence-specific assignments and secondary structure.

Wildegger, G. and Bentrop, D. and Ejchart, A. and Alber, M. and Hage, A. and Sterner, Reinhard and Rösch, P. (1995) 1H nuclear-magnetic-resonance investigation of oxidized Fe4S4 ferredoxin from Thermotoga maritima. Hyperfine-shifted resonances, sequence-specific assignments and secondary structure. European journal of biochemistry / FEBS 229 (3), pp. 658-68.

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Abstract

The oxidized Fe4S4 ferredoxin from the hyperthermophilic bacterium Thermotoga maritima has been investigated by one- and two-dimensional NMR in order to characterize its hyperfine-shifted resonances originating from the cysteinyl cluster ligands and to assign its resonances in the diamagnetic shift range. The chemical shift and relaxation time pattern of the hyperfine-shifted signals is very ...

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Item Type:Article
Date:1995
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
7758460PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
Cysteine/chemistryMESH
Ferredoxins/chemistryMESH
Gram-Negative Anaerobic Bacteria/chemistryMESH
Iron-Sulfur Proteins/chemistryMESH
Magnetic Resonance SpectroscopyMESH
Molecular Sequence DataMESH
Oxidation-ReductionMESH
Protein FoldingMESH
Protein Structure, SecondaryMESH
Sequence AlignmentMESH
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 09:35
Last Modified:22 Mar 2010 09:35
Item ID:13716
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