2006 - Fellow of the American Association for the Advancement of Science (AAAS)
1971 - Fellow of John Simon Guggenheim Memorial Foundation
His main research concerns Biochemistry, Stereochemistry, Active site, Amino acid and Site-directed mutagenesis. His study in Pyridoxal phosphate, Enzyme and Binding site is carried out as part of his Biochemistry studies. His studies deal with areas such as Hydrolysis and Catalysis as well as Enzyme.
The Stereochemistry study combines topics in areas such as Cationic polymerization and Mutagenesis, Mutant. The various areas that he examines in his Amino acid study include Mutation and Peptide sequence. The study incorporates disciplines such as Mutagenesis, Wild type and Transamination in addition to Site-directed mutagenesis.
Jack F. Kirsch spends much of his time researching Stereochemistry, Biochemistry, Enzyme, Active site and Enzyme kinetics. His Stereochemistry research incorporates themes from Amino acid, Transamination, Pyridoxal phosphate, Substrate and ATP synthase. His study looks at the relationship between Amino acid and topics such as Site-directed mutagenesis, which overlap with Mutagenesis.
His Biochemistry study frequently links to adjacent areas such as Molecular biology. His Enzyme study incorporates themes from Mutant and Escherichia coli. Jack F. Kirsch works mostly in the field of Enzyme kinetics, limiting it down to topics relating to Catalysis and, in certain cases, Papain, as a part of the same area of interest.
Biochemistry, Stereochemistry, Escherichia coli, Enzyme and Genetics are his primary areas of study. His research integrates issues of Crystallography, Pyridoxal, Cofactor and Protein secondary structure in his study of Stereochemistry. His Escherichia coli research includes themes of Pyridoxal phosphate, Denaturation and Lactate dehydrogenase.
Jack F. Kirsch studies Enzyme, focusing on Active site in particular. His Genetics research focuses on subjects like Computational biology, which are linked to Exome sequencing, Exome, Newborn screening and DNA. His Enzyme kinetics study combines topics in areas such as Amino acid, Catalysis, Tyrosinemia and Clostridium perfringens.
Jack F. Kirsch mainly focuses on Crystallography, Sequence analysis, Protein structure, Binding site and Inhibitor protein. His Crystallography study combines topics from a wide range of disciplines, such as Mass spectrometry, Electrospray ionization, Analytical chemistry and Dissociation. His Sequence analysis research includes themes of Proteomics methods and Active site.
His Protein structure study integrates concerns from other disciplines, such as Peptide sequence, Mutant, Point mutation and Supplementary data. His research on Peptide sequence focuses in particular on Sequence alignment. Jack F. Kirsch has researched Binding site in several fields, including Conformational isomerism, Protein engineering, Salt bridge and Protein–protein interaction.
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Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Andrew C. Eliot;Jack F. Kirsch.
Annual Review of Biochemistry (2003)
Direct Bronsted analysis of the restoration of activity to a mutant enzyme by exogenous amines
Michael D. Toney;Jack F. Kirsch.
Autoinhibition of human dicer by its internal helicase domain.
Enbo Ma;Ian J. MacRae;Jack F. Kirsch;Jennifer A. Doudna.
Journal of Molecular Biology (2008)
Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing.
Bruce A. Malcolm;Keith P. Wilson;Brian W. Matthews;Jack F. Kirsch;Jack F. Kirsch.
Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation.
Antoon C. Brouwer;Jack F. Kirsch.
Site-directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme
B A Malcolm;S Rosenberg;M J Corey;J S Allen.
Proceedings of the National Academy of Sciences of the United States of America (1989)
Energetic analysis of an antigen/antibody interface: Alanine scanning mutagenesis and double mutant cycles on the hyhel‐10/lysozyme interaction
Jaume Pons;Arvind Rajpal;Jack F. Kirsch.
Protein Science (1999)
Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase.
Michael Bazelyansky;Ellen Robey;Jack F. Kirsch.
Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.
James J. Onuffer;Jack F. Kirsch.
Protein Science (1995)
Nonlinear Structure-Reactivity Correlations. The Imidazole-Catalyzed Hydrolysis of Esters
Jack F. Kirsch;William P. Jencks.
Journal of the American Chemical Society (1964)
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