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.
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.
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.
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.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
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.
M T Stubbs;B Laber;W Bode;R Huber.
The EMBO Journal (1990)
A player of many parts : the spotlight falls on thrombin's structure
Milton T. Stubbs;Milton T. Stubbs;Wolfram Bode;Wolfram Bode.
Thrombosis Research (1993)
Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases.
Jürgen J. May;Nadine Kessler;Mohamed A. Marahiel;Milton T. Stubbs.
Proceedings of the National Academy of Sciences of the United States of America (2002)
Crystal structures of the membrane-binding C2 domain of human coagulation factor V.
Sandra Macedo-Ribeiro;Wolfram Bode;Robert Huber;Mary Ann Quinn-Allen.
Structural basis for the cyclization of the lipopeptide antibiotic surfactin by the thioesterase domain SrfTE.
Steven D Bruner;Thomas Weber;Rahul M Kohli;Dirk Schwarzer.
The interaction of thrombin with fibrinogen. A structural basis for its specificity.
Milton T. Stubbs;Hartmut Oschkinat;Irmgard Mayr;Robert Huber.
FEBS Journal (1992)
The ornithodorin-thrombin crystal structure, a key to the TAP enigma?
A. van de Locht;M. T. Stubbs;W. Bode;T. Friedrich.
The EMBO Journal (1996)
Passing the baton in class B GPCRs: peptide hormone activation via helix induction?
Christoph Parthier;Steffen Reedtz-Runge;Rainer Rudolph;Milton T. Stubbs.
Trends in Biochemical Sciences (2009)
The clot thickens: clues provided by thrombin structure
Milton T. Stubbs;Wolfram Bode.
Trends in Biochemical Sciences (1995)
Crystal Structure of the Nucleotide-binding Domain of the ABC-transporter Haemolysin B: Identification of a Variable Region Within ABC Helical Domains
Lutz Schmitt;Houssain Benabdelhak;Mark A. Blight;I.Barry Holland.
Journal of Molecular Biology (2003)
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