His primary scientific interests are in Protein structure, Crystallography, Nuclear magnetic resonance spectroscopy, Stereochemistry and Biochemistry. His work carried out in the field of Protein structure brings together such families of science as Biophysics, Structural biology, Peptide sequence and Binding site. Masatsune Kainosho combines subjects such as Transmembrane domain and Talos with his study of Structural biology.
His Crystallography study combines topics in areas such as Isotopic labeling, Magnetic dipole–dipole interaction, Phase and NMR spectra database. His studies deal with areas such as Fullerene, Thio-, G protein and Physical chemistry as well as Nuclear magnetic resonance spectroscopy. His study looks at the relationship between Stereochemistry and fields such as Carbon, as well as how they intersect with chemical problems.
Masatsune Kainosho spends much of his time researching Stereochemistry, Crystallography, Nuclear magnetic resonance spectroscopy, Biochemistry and Amino acid. As a member of one scientific family, Masatsune Kainosho mostly works in the field of Stereochemistry, focusing on Chemical shift and, on occasion, Amide. Masatsune Kainosho interconnects Dihedral angle, Hydrogen bond, Heteronuclear single quantum coherence spectroscopy, NMR spectra database and Protein structure in the investigation of issues within Crystallography.
Protein structure is closely attributed to Structural biology in his study. In Nuclear magnetic resonance spectroscopy, Masatsune Kainosho works on issues like Analytical chemistry, which are connected to Spinning. The Amino acid study combines topics in areas such as Residue, Methyl group and Protein biosynthesis.
Biochemistry, Amino acid, Stereochemistry, Nuclear magnetic resonance spectroscopy and Chemical shift are his primary areas of study. His Amino acid study integrates concerns from other disciplines, such as Arabidopsis, Mutant and Phylogenetic tree. Stereochemistry and DsbA are two areas of study in which he engages in interdisciplinary research.
His Nuclear magnetic resonance spectroscopy study combines topics from a wide range of disciplines, such as Conformational isomerism, Atom and Chemical structure. His studies in Chemical shift integrate themes in fields like Oxidoreductase and Cyana, Two-dimensional nuclear magnetic resonance spectroscopy. His work in Heteronuclear molecule addresses issues such as Computational chemistry, which are connected to fields such as Hydrogen bond.
The scientist’s investigation covers issues in Amino acid, Mutant, Biochemistry, Protonation and Solid-state nuclear magnetic resonance. The concepts of his Amino acid study are interwoven with issues in Stereochemistry, A protein and Phylogenetic tree. His Mutant research incorporates elements of Dehydratase, Biosynthesis and Enzyme.
Many of his research projects under Biochemistry are closely connected to Malate synthase with Malate synthase, tying the diverse disciplines of science together. The various areas that Masatsune Kainosho examines in his Protonation study include Mole, Spinning and Analytical chemistry.
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NMR characterization of isomers of C 78 , C 82 and C 84 fullerenes
Koichi Kikuchi;Nobuo Nakahara;Tomonari Wakabayashi;Shinzo Suzuki.
Optimal isotope labelling for NMR protein structure determinations
Masatsune Kainosho;Takuya Torizawa;Yuki Iwashita;Tsutomu Terauchi.
NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy
Konstantin Pervushin;Akira Ono;César Fernández;Thomas Szyperski.
Proceedings of the National Academy of Sciences of the United States of America (1998)
NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ
Toshiyuki Tanaka;Soumitra K. Saha;Chieri Tomomori;Rieko Ishima.
Well-Controlled Polymerization of Phenylacetylenes with Organorhodium(I) Complexes: Mechanism and Structure of the Polyenes
Yasuhisa Kishimoto;Peter Eckerle;Tatsuya Miyatake;Masatsune Kainosho.
Journal of the American Chemical Society (1999)
The NMR Structure of a DNA Dodecamer in an Aqueous Dilute Liquid Crystalline Phase
Nico Tjandra;Shin-ichi Tate;Akira Ono;Masatsune Kainosho.
Journal of the American Chemical Society (2000)
Assignment of the three methionyl carbonyl carbon resonances in Streptomyces subtilisin inhibitor by a carbon-13 and nitrogen-15 double-labeling technique. A new strategy for structural studies of proteins in solution.
Masatsune Kainosho;Takashi Tsuji.
Solution NMR structure of proteorhodopsin.
Sina Reckel;Daniel Gottstein;Jochen Stehle;Frank Löhr.
Angewandte Chemie (2011)
Structural details on mdm2-p53 interaction.
Seung-Wook Chi;Si-Hyung Lee;Do-Hyoung Kim;Min-Jung Ahn.
Journal of Biological Chemistry (2005)
Efficient production of isotopically labeled proteins by cell-free synthesis: a practical protocol.
Takuya Torizawa;Masato Shimizu;Masato Taoka;Hiroshi Miyano.
Journal of Biomolecular NMR (2004)
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