What is he best known for?
The fields of study he is best known for:
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.
His most cited work include:
- Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. (603 citations)
- Autoinhibition of human dicer by its internal helicase domain. (173 citations)
- Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing. (159 citations)
What are the main themes of his work throughout his whole career to date?
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.
He most often published in these fields:
- Stereochemistry (48.65%)
- Biochemistry (33.78%)
- Enzyme (32.43%)
What were the highlights of his more recent work (between 2004-2020)?
- Biochemistry (33.78%)
- Stereochemistry (48.65%)
- Escherichia coli (12.84%)
In recent papers he was focusing on the following fields of study:
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.
Between 2004 and 2020, his most popular works were:
- Autoinhibition of human dicer by its internal helicase domain. (173 citations)
- Active site prediction using evolutionary and structural information (58 citations)
- The Enzymology of Cystathionine Biosynthesis: Strategies for the Control of Substrate and Reaction Specificity (48 citations)
In his most recent research, the most cited papers focused on:
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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