1974 - Fellow of the American Academy of Arts and Sciences
1973 - Member of the National Academy of Sciences
His scientific interests lie mostly in Enzyme, Biochemistry, Stereochemistry, Biophysics and Physical chemistry. His Enzyme study contributes to a more complete understanding of Organic chemistry. Gordon G. Hammes works mostly in the field of Biochemistry, limiting it down to topics relating to Uracil nucleotide and, in certain cases, Spectrophotometry and Phosphate, as a part of the same area of interest.
His Stereochemistry study combines topics from a wide range of disciplines, such as Fluorescence, Active site, Dihydrofolate reductase, Dissociation constant and Protein structure. The Biophysics study combines topics in areas such as Oxidative phosphorylation, Macromolecule, Membrane, Chromatography and Phosphorylation. His Physical chemistry study combines topics in areas such as Rate equation, Reaction rate constant, Relaxation spectrometry and Substrate.
His main research concerns Biochemistry, Stereochemistry, Enzyme, Biophysics and Binding site. His research ties Fluorescence and Biochemistry together. His research in Stereochemistry intersects with topics in Reaction rate constant, Fatty acid synthase, Förster resonance energy transfer, Dissociation constant and Aspartate Transcarbamylase.
His Aspartate Transcarbamylase study frequently draws connections between related disciplines such as Relaxation. His Enzyme research incorporates elements of Conformational change and Catalysis. His Biophysics study integrates concerns from other disciplines, such as Membrane and Coupling.
Gordon G. Hammes mostly deals with Enzyme, Biochemistry, Stereochemistry, Biophysics and DNA polymerase. His Molecule research extends to the thematically linked field of Enzyme. His work in Biochemistry tackles topics such as Molecular biology which are related to areas like Yeast and Vesicle-associated membrane protein 8.
He has included themes like Enzyme catalysis, Quenching, Dihydrofolate reductase, Protein structure and Phosphorescence in his Stereochemistry study. As part of the same scientific family, Gordon G. Hammes usually focuses on Dihydrofolate reductase, concentrating on Conformational change and intersecting with Biotin, Dissociation constant and Flavin mononucleotide. Vesicle and Phospholipid is closely connected to Fluorescence in his research, which is encompassed under the umbrella topic of Biophysics.
His scientific interests lie mostly in Enzyme, Stereochemistry, Dihydrofolate reductase, Protein structure and Enzyme catalysis. Enzyme is a primary field of his research addressed under Biochemistry. His Stereochemistry research includes themes of Reaction rate constant, Biophysics, Molecule and Active site.
The concepts of his Dihydrofolate reductase study are interwoven with issues in Conformational change, Fluorescence, Substrate and Dissociation constant. His Protein structure research is multidisciplinary, incorporating elements of Chemical physics, Crystallography, Protein folding and Ligand. His study focuses on the intersection of Enzyme catalysis and fields such as Computational chemistry with connections in the field of Catalysis, Allosteric enzyme, Primary, Aspartate carbamoyltransferase and Allosteric regulation.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Conformational selection or induced fit: A flux description of reaction mechanism
Gordon G. Hammes;Yu Chu Chang;Terrence G. Oas.
Proceedings of the National Academy of Sciences of the United States of America (2009)
Application of the Theory of Diffusion-controlled Reactions to Enzyme Kinetics
Robert A. Alberty;Gordon G. Hammes.
The Journal of Physical Chemistry (1958)
Multiple Conformational Changes in Enzyme Catalysis
Gordon G. Hammes.
Interaction of dihydrofolate reductase with methotrexate: Ensemble and single-molecule kinetics
P. T. Ravi Rajagopalan;Zhiquan Zhang;Lynn McCourt;Mary Dwyer.
Proceedings of the National Academy of Sciences of the United States of America (2002)
Free-Energy Landscape of Enzyme Catalysis†
Stephen J. Benkovic;Gordon G. Hammes;Sharon Hammes-Schiffer.
Calculation on fluorescence resonance energy transfer on surfaces
T.G. Dewey;G.G. Hammes.
Biophysical Journal (1980)
Further characterization of nucleotide binding sites on chloroplast coupling factor one.
Michael F. Bruist;Gordon G. Hammes.
Flexibility, Diversity, and Cooperativity: Pillars of Enzyme Catalysis
Gordon G. Hammes;Stephen J. Benkovic;Sharon Hammes-Schiffer.
Binding of phosphate ligands to ribonuclease A.
David G. Anderson;Gordon G. Hammes;Frederick G. Walz.
Relaxation spectrometry of biological systems.
Gordon G. Hammes.
Advances in Protein Chemistry (1968)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: