D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Chemistry D-index 75 Citations 19,343 327 World Ranking 2620 National Ranking 211

Research.com Recognitions

Awards & Achievements

Member of the European Molecular Biology Organization (EMBO)

Overview

What is he best known for?

The fields of study he is best known for:

  • Gene
  • Enzyme
  • Amino acid

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.

His most cited work include:

  • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy (730 citations)
  • Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin. (397 citations)
  • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide (368 citations)

What are the main themes of his work throughout his whole career to date?

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.

He most often published in these fields:

  • Crystallography (22.92%)
  • Nuclear magnetic resonance spectroscopy (20.92%)
  • Biochemistry (19.48%)

What were the highlights of his more recent work (between 2013-2021)?

  • Biophysics (14.61%)
  • Nuclear magnetic resonance spectroscopy (20.92%)
  • Magic angle spinning (12.61%)

In recent papers he was focusing on the following fields of study:

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.

Between 2013 and 2021, his most popular works were:

  • AhR sensing of bacterial pigments regulates antibacterial defence (208 citations)
  • Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning (161 citations)
  • Theoretical aspects of Magic Angle Spinning - Dynamic Nuclear Polarization. (54 citations)

In his most recent research, the most cited papers focused on:

  • Gene
  • Enzyme
  • Amino acid

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.

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.

Best Publications

Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

Federica Castellani;Barth van Rossum;Annette Diehl;Mario Schubert.
Nature (2002)

1042 Citations

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.
Nature (1996)

544 Citations

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)

537 Citations

Perspectives on NMR in drug discovery: a technique comes of age

Maurizio Pellecchia;Ivano Bertini;David Cowburn;Claudio Dalvit.
Nature Reviews Drug Discovery (2008)

430 Citations

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)

428 Citations

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)

405 Citations

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)

398 Citations

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.
ChemBioChem (2001)

378 Citations

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)

344 Citations

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)

318 Citations

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