The conserved Cys76 plays a crucial role for the conformation of reduced glutathione peroxidase-type tryparedoxin peroxidase

FEBS Letters

Volumn 584, Issue 5, 2010, Pages 1027-1032

  Muhle Goll, Claudia ^a   Füller, Florian ^b   Ulrich, Anne S ^a   Luise Krauth Siegel, R ^b  

^a KARLSRUHE INSTITUTE OF TECHNOLOGY   (Germany)

^b UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

Glutathione peroxidase; Protein structure; Trypanosoma brucei; Trypanothione; Tryparedoxin

Indexed keywords

CYSTEINE; GLUTAMINE; GLUTATHIONE PEROXIDASE; REDUCED TRYPAREDOXIN PEROXIDASE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CIRCULAR DICHROISM; CONSERVATION BIOLOGY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME METABOLISM; FLUORESCENCE ANALYSIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; RESIDUE ANALYSIS; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION; WILD TYPE;

ANIMALS; CIRCULAR DICHROISM; CYSTEINE; MAGNETIC RESONANCE SPECTROSCOPY; PEROXIDASES; PROTEIN STRUCTURE, SECONDARY; PROTOZOAN PROTEINS; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP;

TRYPANOSOMA BRUCEI;

EID: 76749136135     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.01.054     Document Type: Article

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