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Identification of a novel archaebacterial thioredoxin: determination of function through structure.

Bhattacharyya S, Habibi-Nazhad B, Amegbey G, Slupsky CM, Yee A, Arrowsmith C, Wishart DS,
Biochemistry (2002) 41(15):4760-70 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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As part of a high-throughput, structural proteomic project we have used NMR spectroscopy to determine the solution structure and ascertain the function of a previously unknown, conserved protein (MtH895) from the thermophilic archeon Methanobacterium thermoautotrophicum. ...
metabolism chemistry 
Binding Sites Amino Acid Sequence Conserved Sequence Models, Molecular Molecular Sequence Data Sequence Alignment Protein Conformation Methanobacterium Solutions Magnetic Resonance Spectroscopy Thioredoxins Thermodynamics DNA-Directed DNA Polymerase 
22 (Last update: 01/19/2019 7:22:30pm)  
Biochemistry. 2002 Apr 16;41(15):4760-70.