What is he best known for?
The fields of study he is best known for:
The scientist’s investigation covers issues in Biochemistry, Ultracentrifuge, Aspartate carbamoyltransferase, Stereochemistry and Sedimentation equilibrium.
His study in the fields of Aspartate Transcarbamylase, Enzymatic synthesis and Deoxyadenine Nucleotides under the domain of Biochemistry overlaps with other disciplines such as Thymidine monophosphate.
His Ultracentrifuge study combines topics from a wide range of disciplines, such as Rayleigh scattering, Optics, Centrifugation and Analytical chemistry.
Howard K. Schachman combines subjects such as Protein structure, Protein sequencing, Sedimentation coefficient and Circular permutation in proteins with his study of Aspartate carbamoyltransferase.
The concepts of his Stereochemistry study are interwoven with issues in Dissociation, Titration, Side chain, Chaotropic agent and Order of reaction.
His research in Sedimentation equilibrium tackles topics such as Molecular mass which are related to areas like Redistribution, Molecule and Myoglobin.
His most cited work include:
- Ultracentrifugation in biochemistry (874 citations)
- Distinct Subunits for the Regulation and Catalytic Activity of Aspartate Transcarbamylase (452 citations)
- The Simultaneous Determination of Partial Specific Volumes and Molecular Weights with Microgram Quantities (334 citations)
What are the main themes of his work throughout his whole career to date?
His main research concerns Aspartate carbamoyltransferase, Biochemistry, Stereochemistry, Allosteric regulation and Enzyme.
The Aspartate carbamoyltransferase study combines topics in areas such as Protein structure, Protein subunit, Trimer and Active site.
His study in Mutant, Ultracentrifuge, Structural gene, Aspartate Transcarbamylase and DNA is carried out as part of his studies in Biochemistry.
His work deals with themes such as Rayleigh scattering and Analytical chemistry, which intersect with Ultracentrifuge.
In his work, Site-directed mutagenesis is strongly intertwined with Amino acid, which is a subfield of Stereochemistry.
His work on Allosteric enzyme as part of general Allosteric regulation research is frequently linked to Ligand, bridging the gap between disciplines.
He most often published in these fields:
- Aspartate carbamoyltransferase (47.57%)
- Biochemistry (38.35%)
- Stereochemistry (33.98%)
What were the highlights of his more recent work (between 1990-2016)?
- Aspartate carbamoyltransferase (47.57%)
- Stereochemistry (33.98%)
- Allosteric regulation (22.82%)
In recent papers he was focusing on the following fields of study:
His primary areas of study are Aspartate carbamoyltransferase, Stereochemistry, Allosteric regulation, Trimer and Biochemistry.
His Aspartate carbamoyltransferase study is concerned with Enzyme in general.
His Stereochemistry research includes elements of Reaction mechanism, Cooperativity, Holoenzymes and Active site.
His studies examine the connections between Allosteric regulation and genetics, as well as such issues in Protein engineering, with regards to Protein folding.
His research in Trimer intersects with topics in Conformational change, Denaturation and Aspartic acid.
His study in Nucleotide, Structural gene, Protein tertiary structure and Escherichia coli is carried out as part of his Biochemistry studies.
Between 1990 and 2016, his most popular works were:
- Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase (120 citations)
- A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase (80 citations)
- In Vivo Formation of Allosteric Aspartate Transcarbamoylase Containing Circularly Permuted Catalytic Polypeptide Chains: Implications for Protein Folding and Assembly (54 citations)
In his most recent research, the most cited papers focused on:
His scientific interests lie mostly in Aspartate carbamoyltransferase, Stereochemistry, Allosteric regulation, Active site and Enzyme.
His Aspartate carbamoyltransferase course of study focuses on Circular permutation in proteins and Protein folding and Cooperativity.
Howard K. Schachman interconnects Protein structure, Trimer and Molecular systems in the investigation of issues within Stereochemistry.
His Allosteric regulation study combines topics in areas such as Amino acid, Protein engineering and Binding site.
His research in Active site focuses on subjects like Allosteric enzyme, which are connected to Cytidine triphosphate, Nucleotide and Transferase.
His studies deal with areas such as Protein subunit and Aspartic acid as well as Enzyme.
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