1968 - Member of the National Academy of Sciences
1966 - Fellow of the American Association for the Advancement of Science (AAAS)
1956 - Fellow of John Simon Guggenheim Memorial Foundation
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 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.
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.
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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Ultracentrifugation in biochemistry
Howard K Schachman.
Distinct Subunits for the Regulation and Catalytic Activity of Aspartate Transcarbamylase
John C. Gerhart;Howard K. Schachman.
Enzymatic synthesis of deoxyribonucleic acid. VII. Synthesis of a polymer of deoxyadenylate and deoxythymidylate
H. K. Schachman;H. K. Schachman;H. K. Schachman;Julius Adler;Julius Adler;Julius Adler;Charles M. Radding;Charles M. Radding;Charles M. Radding;I. R. Lehman;I. R. Lehman;I. R. Lehman.
Journal of Biological Chemistry (1960)
Ultracentrifuge studies with absorption optics. IV. Molecular weight determinations at the microgram level.
H. K. Schachman;S. J. Edelstein.
Ultracentrifuge Studies with Rayleigh Interference Optics.I. General Application
E Glen Richards;Howard K. Schachman.
The Journal of Physical Chemistry (1959)
Allosteric Interactions in Aspartate Transcarbamylase. II. Evidence for Different Conformational States of the Protein in the Presence and Absence of Specific Ligands
John C. Gerhart;Howard K. Schachman.
The Simultaneous Determination of Partial Specific Volumes and Molecular Weights with Microgram Quantities
S.J. Edelstein;H.K. Schachman.
Journal of Biological Chemistry (1967)
Studies on the macro-molecular organization of microbial cells.
Howard K. Schachman;Arthur B. Pardee;Roger Y. Stanier.
Archives of Biochemistry and Biophysics (1952)
STUDIES ON BODY COMPOSITION IV. USE OF RADIOACTIVE HYDROGEN FOR MEASUREMENT IN VIVO OF TOTAL BODY WATER
Nello Pace;Leo Kline;Howard K. Schachman;Morton Harfenist.
Journal of Biological Chemistry (1945)
Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits.
Jean P. Changeux;John C. Gerhart;Howard K. Schachman.
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