The scientist’s investigation covers issues in Biochemistry, Stereochemistry, Enzyme, Binding site and Isocitrate dehydrogenase. Biochemistry is a component of his Chemotaxis, Phosphorylation, Citric acid cycle, Branched-chain alpha-keto acid dehydrogenase complex and Allosteric regulation studies. Within one scientific family, he focuses on topics pertaining to Cysteine under Stereochemistry, and may sometimes address concerns connected to Aspartate binding.
His biological study deals with issues like Ultrasensitivity, which deal with fields such as Covalent modification. His Binding site research incorporates themes from Protein structure, Plasma protein binding, Protein subunit and Cooperativity. His work deals with themes such as Allosteric enzyme, Isocitrate lyase, IDH1 and Active site, which intersect with Isocitrate dehydrogenase.
His primary scientific interests are in Biochemistry, Chemotaxis, Enzyme, Stereochemistry and Receptor. His Biochemistry research includes themes of Molecular biology and Biophysics. His Chemotaxis research integrates issues from Mutant, Gene, Salmonella, Bacteria and Cell biology.
The various areas that Daniel E. Koshland examines in his Stereochemistry study include Isocitrate dehydrogenase, Ligand, Active site, Substrate and Binding site. As part of his studies on Isocitrate dehydrogenase, Daniel E. Koshland often connects relevant subjects like IDH1. His study ties his expertise on Protein structure together with the subject of Binding site.
His scientific interests lie mostly in Biochemistry, Stereochemistry, Binding site, Receptor and Enzyme. His study involves Mutant, Escherichia coli, Periplasmic space, Mutagenesis and Serine, a branch of Biochemistry. In his study, Molecular biology is inextricably linked to Methylation, which falls within the broad field of Escherichia coli.
His research integrates issues of Isocitrate dehydrogenase, Ligand, Active site, Substrate and Stereospecificity in his study of Stereochemistry. His study in Binding site is interdisciplinary in nature, drawing from both Plasma protein binding, Crystallography, Protein subunit, Aspartic acid and Protein structure. His Receptor study integrates concerns from other disciplines, such as Cytoplasm, Cooperativity and Cooperative binding.
Daniel E. Koshland mainly focuses on Stereochemistry, Biochemistry, Binding site, Receptor and Enzyme. Daniel E. Koshland combines subjects such as Isocitrate dehydrogenase, Ligand, Protein subunit, Active site and Substrate with his study of Stereochemistry. His Biochemistry study focuses mostly on Sialic acid, Phosphorylation, Peptide, MAP kinase cascade and Cell.
He has researched Binding site in several fields, including Aspartic acid, Cysteine, Protein structure, Aspartate carbamoyltransferase and Conformational change. The Receptor study combines topics in areas such as Cooperative binding, Cooperativity and Escherichia coli. His studies deal with areas such as Value and Constant as well as Enzyme.
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Comparison of experimental binding data and theoretical models in proteins containing subunits.
D. E. Koshland;G. Némethy;D. Filmer.
Application of a Theory of Enzyme Specificity to Protein Synthesis
Proceedings of the National Academy of Sciences of the United States of America (1958)
An amplified sensitivity arising from covalent modification in biological systems
Albert Goldbeter;Daniel E. Koshland.
Proceedings of the National Academy of Sciences of the United States of America (1981)
A Method for the Quantitative Modification and Estimation of Carboxylic Acid Groups in Proteins
D.G. Hoare;D.E. Koshland.
Journal of Biological Chemistry (1967)
STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS
D. E. Koshland.
Biological Reviews (1953)
The Gradient-Sensing Mechanism in Bacterial Chemotaxis
Robert M. Macnab;D. E. Koshland.
Proceedings of the National Academy of Sciences of the United States of America (1972)
NO news is good news
Elizabeth Culotta;Daniel E. Koshland.
The molecule of the year.
Daniel E. Koshland.
The Key–Lock Theory and the Induced Fit Theory
Daniel E. Koshland.
Angewandte Chemie (1995)
Negative cooperativity in enzyme action. Binding of diphosphopyridine nucleotide to glyceraldehyde-3-phosphate dehydrogenase
Abby. Conway;Daniel E. Koshland.
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