What is he best known for?
The fields of study he is best known for:
His main research concerns Stereochemistry, Biochemistry, Protein structure, Binding site and Active site.
His Stereochemistry course of study focuses on Carbonic anhydrase and Moiety, Sulfonamide and Hydrogen bond.
Biochemistry is closely attributed to Biophysics in his research.
His research integrates issues of GPR119, Nonribosomal peptide and Surfactin in his study of Protein structure.
His Binding site research includes elements of Benzamidine and Plasma protein binding.
The study incorporates disciplines such as Peptide sequence, Protease and Protein domain in addition to Active site.
His most cited work include:
- The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. (417 citations)
- A player of many parts : the spotlight falls on thrombin's structure (380 citations)
- A player of many parts : the spotlight falls on thrombin's structure (380 citations)
What are the main themes of his work throughout his whole career to date?
The scientist’s investigation covers issues in Biochemistry, Stereochemistry, Protein structure, Crystallography and Binding site.
Enzyme, Active site, Peptide sequence, Transferase and Recombinant DNA are the core of his Biochemistry study.
His Stereochemistry study integrates concerns from other disciplines, such as Hydrolase, Transfer RNA, Chemical synthesis and Trypsin.
Milton T. Stubbs has researched Trypsin in several fields, including Benzamidine, Selectivity and Factor Xa Inhibitor.
His work deals with themes such as Plasma protein binding and Nuclear magnetic resonance spectroscopy, which intersect with Protein structure.
His Binding site research is multidisciplinary, relying on both Pharmacophore, Amino acid and Ligand.
He most often published in these fields:
- Biochemistry (43.31%)
- Stereochemistry (42.68%)
- Protein structure (21.02%)
What were the highlights of his more recent work (between 2010-2021)?
- Biochemistry (43.31%)
- Stereochemistry (42.68%)
- Protein structure (21.02%)
In recent papers he was focusing on the following fields of study:
Milton T. Stubbs mostly deals with Biochemistry, Stereochemistry, Protein structure, Crystallography and Enzyme.
Milton T. Stubbs integrates many fields in his works, including Stereochemistry and Exoribonuclease.
His Protein structure research includes themes of Fibril, Peptide sequence and Nuclear magnetic resonance spectroscopy.
Milton T. Stubbs has included themes like Monolayer, Nanotechnology, Glutaminyl cyclase and Biotinylation in his Crystallography study.
His work on Enzyme structure as part of general Enzyme study is frequently linked to Tannerella forsythia, therefore connecting diverse disciplines of science.
His study in Hydrolase is interdisciplinary in nature, drawing from both Substrate, Enzyme catalysis, Binding site and Trypsin.
Between 2010 and 2021, his most popular works were:
- Molecular basis of β-amyloid oligomer recognition with a conformational antibody fragment (59 citations)
- The O-carbamoyltransferase TobZ catalyzes an ancient enzymatic reaction. (45 citations)
- N-terminal protein modification by substrate-activated reverse proteolysis. (36 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Biochemistry, Protein structure, Enzyme, Peptide and Fibril.
He combines Protein structure and Low protein in his studies.
He interconnects Biocatalysis and Bioconjugation in the investigation of issues within Enzyme.
His studies deal with areas such as Complementarity determining region and Peptide sequence as well as Fibril.
His studies in Transferase integrate themes in fields like Tryptophan, Crystal structure, Active center, Cysteine and Stereochemistry.
His study with Binding domain involves better knowledge in Binding site.
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