Member of the European Molecular Biology Organization (EMBO)
His scientific interests lie mostly in Crystallography, Solid-state nuclear magnetic resonance, Protein structure, Two-dimensional nuclear magnetic resonance spectroscopy and Magic angle spinning. His Crystallography research is multidisciplinary, incorporating perspectives in Chaperone, Peptide sequence, Nuclear magnetic resonance spectroscopy, Side chain and Chemical shift. The Nuclear magnetic resonance spectroscopy study combines topics in areas such as Biophysics and NMR spectra database.
In his study, Coherence, Polarization, Spinning and Intensity is strongly linked to Analytical chemistry, which falls under the umbrella field of Solid-state nuclear magnetic resonance. His Protein structure research incorporates elements of Nuclear magnetic resonance spectroscopy of nucleic acids, Polyproline helix, Stereochemistry and Protein secondary structure. His Two-dimensional nuclear magnetic resonance spectroscopy research includes elements of Pulse sequence and Homonuclear molecule.
Hartmut Oschkinat mostly deals with Crystallography, Nuclear magnetic resonance spectroscopy, Biochemistry, Stereochemistry and Analytical chemistry. His research integrates issues of Protein secondary structure, Solid-state nuclear magnetic resonance, Heteronuclear molecule, Protein structure and Chemical shift in his study of Crystallography. His study in Solid-state nuclear magnetic resonance is interdisciplinary in nature, drawing from both Magic angle spinning and Membrane protein.
Nuclear magnetic resonance spectroscopy is closely attributed to Two-dimensional nuclear magnetic resonance spectroscopy in his work. His Biochemistry study frequently draws connections to adjacent fields such as Biophysics. His studies in Stereochemistry integrate themes in fields like Amino acid, Side chain, Protein domain and WW domain.
His primary areas of investigation include Biophysics, Nuclear magnetic resonance spectroscopy, Magic angle spinning, Solid-state nuclear magnetic resonance and Analytical chemistry. In the subject of general Biophysics, his work in Fibril is often linked to Protonation, thereby combining diverse domains of study. Hartmut Oschkinat has included themes like Crystallography, Photochemistry, Electron paramagnetic resonance, Conformational isomerism and Radical in his Nuclear magnetic resonance spectroscopy study.
He integrates several fields in his works, including Crystallography and Outer membrane protein G. His Magic angle spinning study incorporates themes from Polarization and Amide. His research in Solid-state nuclear magnetic resonance intersects with topics in Resolution, Computational chemistry, Two-dimensional nuclear magnetic resonance spectroscopy and Substrate.
Hartmut Oschkinat mainly focuses on Nuclear magnetic resonance spectroscopy, Magic angle spinning, Analytical chemistry, Biophysics and Solid-state nuclear magnetic resonance. As a part of the same scientific study, Hartmut Oschkinat usually deals with the Nuclear magnetic resonance spectroscopy, concentrating on Peptide and frequently concerns with Cleavage. His Magic angle spinning research is included under the broader classification of Nuclear magnetic resonance.
His research investigates the connection between Analytical chemistry and topics such as Spinning that intersect with problems in Chemical physics and Microcrystalline. His biological study spans a wide range of topics, including Resolution and Two-dimensional nuclear magnetic resonance spectroscopy. His research investigates the link between NMR spectra database and topics such as Relaxation that cross with problems in Conformational isomerism, Protein structure, Molecule, Intermolecular force and Crystallography.
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Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
Federica Castellani;Barth van Rossum;Annette Diehl;Mario Schubert.
Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
Maria J. Macias;Marko Hyvönen;Elena Baraldi;Johan Schultz.
Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin.
Michael Nilges;Maria J Macias;Séan I O’Donoghue;Hartmut Oschkinat.
Journal of Molecular Biology (1997)
Perspectives on NMR in drug discovery: a technique comes of age
Maurizio Pellecchia;Ivano Bertini;David Cowburn;Claudio Dalvit.
Nature Reviews Drug Discovery (2008)
Transformation of homonuclear two-dimensional NMR techniques into one-dimensional techniques using Gaussian pulses
H Kessler;H Oschkinat;C Griesinger;W Bermel.
Journal of Magnetic Resonance (1986)
Structure of the binding site for inositol phosphates in a PH domain.
M Hyvonen;M.J Macias;M Nilges;H Oschkinat.
The EMBO Journal (1995)
Peptide conformations. Part 31. The conformation of cyclosporin a in the crystal and in solution
Hans-Rudolf Loosli;Horst Kessler;Hartmut Oschkinat;Hans-Peter Weber.
Helvetica Chimica Acta (1985)
Backbone and Side-Chain 13C and 15N Signal Assignments of the α-Spectrin SH3 Domain by Magic Angle Spinning Solid-State NMR at 17.6 Tesla
Jutta Pauli;Marc Baldus;Barth van Rossum;Huub de Groot.
A software tool for the prediction of Xaa-Pro peptide bond conformations in proteins based on 13C chemical shift statistics.
Mario Schubert;Dirk Labudde;Hartmut Oschkinat;Peter Schmieder.
Journal of Biomolecular NMR (2002)
Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels.
Johan Schultz;Ulrich Hoffmuüller;Gerd Krause;Jennifer Ashurst.
Nature Structural & Molecular Biology (1998)
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