His primary scientific interests are in Active site, Stereochemistry, Biochemistry, Enzyme and Binding site. The Active site study combines topics in areas such as Protein structure, Carbamoyl phosphate synthetase and Glutamine amidotransferase. His Protein structure research is multidisciplinary, relying on both Crystallography and Ternary complex.
His studies deal with areas such as Hydrolase, Protein subunit, Isomerase, Substrate and NAD+ kinase as well as Stereochemistry. James B. Thoden does research in Enzyme, focusing on Serine specifically. His research in Binding site intersects with topics in Galactokinase deficiency, Mutant protein, Cofactor and Uridine diphosphate glucose.
James B. Thoden focuses on Stereochemistry, Biochemistry, Enzyme, Active site and Protein structure. James B. Thoden has researched Stereochemistry in several fields, including Protein subunit, Carbamoyl phosphate synthetase, Isomerase, Substrate and Binding site. His biological study deals with issues like Campylobacter jejuni, which deal with fields such as Reductase and Microbiology.
His work deals with themes such as Mutant, Protein quaternary structure and Escherichia coli, which intersect with Enzyme. His Active site research includes elements of Amino acid, Crystallography, Hydrolase, Nucleotide and Mutant protein. His study explores the link between Crystallography and topics such as Hydrogen bond that cross with problems in Side chain.
Biochemistry, Enzyme, Stereochemistry, Transferase and Biosynthesis are his primary areas of study. Biochemistry is represented through his Active site, NAD+ kinase, Phosphofructokinase 2, Dehydratase and Structure–activity relationship research. His research integrates issues of Rhamnose, Protein subunit, Giant Virus and Mimivirus in his study of Active site.
He interconnects Escherichia coli, Campylobacter jejuni, Bacteria and Protein quaternary structure in the investigation of issues within Enzyme. James B. Thoden performs integrative study on Stereochemistry and N-acetyltransferase in his works. As a member of one scientific family, he mostly works in the field of Biosynthesis, focusing on Metabolic pathway and, on occasion, Streptomyces, Streptomyces fradiae and Protein tertiary structure.
James B. Thoden focuses on Enzyme, Biochemistry, Transferase, Campylobacter jejuni and Bacteria. The various areas that James B. Thoden examines in his Transferase study include Protein subunit, Pseudomonas aeruginosa, Stereochemistry, Glycoconjugate and Ankyrin repeat. His Protein subunit research integrates issues from Amination, Moiety, Protein structure and Active site.
His research on Stereochemistry often connects related topics like Substrate. His studies in Campylobacter jejuni integrate themes in fields like Pyridoxal, Reductase, Serotype, Microbiology and NAD+ kinase. The concepts of his Bacteria study are interwoven with issues in Phosphofructokinase 2, Protein domain and Escherichia coli.
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X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-.
Andrew J Fisher;Clyde A. Smith;James B. Thoden;Robert Smith.
Structure and Function of Enzymes of the Leloir Pathway for Galactose Metabolism
Hazel M. Holden;Ivan Rayment;James B. Thoden.
Journal of Biological Chemistry (2003)
Structure of carbamoyl phosphate synthetase : a journey of 96 A from substrate to product
James B. Thoden;Hazel M. Holden;Gary Wesenberg;Frank M. Raushel.
X-ray structures of the MgADP, MgATPgammaS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain.
Andrew M. Gulick;Cary B. Bauer;James B. Thoden;Ivan Rayment.
Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center.
James B. Thoden;George N. Phillips;Tamiko M. Neal;Frank M. Raushel.
The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions.
Andrew J. Fisher;Thomas B. Thompson;James B. Thoden;Thomas O. Baldwin.
Journal of Biological Chemistry (1996)
Enzymes with molecular tunnels.
Frank M. Raushel;James B. Thoden;Hazel M. Holden.
Accounts of Chemical Research (2003)
Structural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscle contraction.
A J Fisher;C A Smith;J Thoden;R Smith.
Biophysical Journal (1995)
Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: implications for the catalytic mechanism.
James B. Thoden;Perry A. Frey;Hazel M. Holden.
Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.
James B. Thoden;Travis M. Wohlers;Judith L. Fridovich-Keil;Hazel M. Holden.
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