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Kurt Wüthrich

Researcher Next ID · RN-021249

Researcher · Biochemistry, Genetics and Molecular Biology

Scripps Research Institute

San Diego, Switzerland

Not currently recruitingFunding unknown
Works count
1,000
Citation count
99,120
H-index
144
i10-index
597

Research interests

Biochemistry, Genetics and Molecular Biology
Materials Science
Chemistry
Protein Structure and Dynamics
Enzyme Structure and Function
Advanced NMR Techniques and Applications
Molecular spectroscopy and chirality
Prion Diseases and Protein Misfolding

Publications

  • Attenuated T2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

    WORLD SCIENTIFIC eBooks · 2021 · 10.1142/9789811235795_0006

  • Biased Signaling Pathways in β 2 -Adrenergic Receptor Characterized by 19 F-NMR

    Science · 2012 · 10.1126/science.1215802

  • An EB1-Binding Motif Acts as a Microtubule Tip Localization Signal

    Cell · 2009 · 10.1016/j.cell.2009.04.065

  • Protein NMR Structure Determination with Automated NOE Assignment Using the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA

    Journal of Molecular Biology · 2002 · 10.1016/s0022-2836(02)00241-3

  • NMR solution structure of the human prion protein

    Proceedings of the National Academy of Sciences · 2000 · 10.1073/pnas.97.1.145

  • TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins

    Proceedings of the National Academy of Sciences · 1998 · 10.1073/pnas.95.23.13585

  • Attenuated T 2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

    Proceedings of the National Academy of Sciences · 1997 · https://doi.org/10.1073/pnas.94.23.12366

  • NMR characterization of the full‐length recombinant murine prion protein, mPrP(23–231)

    FEBS Letters · 1997 · 10.1016/s0014-5793(97)00920-4

  • Torsion angle dynamics for NMR structure calculation with the new program Dyana

    Journal of Molecular Biology · 1997 · https://doi.org/10.1006/jmbi.1997.1284

  • NMR structure of the mouse prion protein domain PrP(121–231)

    Nature · 1996 · 10.1038/382180a0

  • MOLMOL: A program for display and analysis of macromolecular structures

    Journal of Molecular Graphics · 1996 · https://doi.org/10.1016/0263-7855(96)00009-4

  • Homeodomain-DNA recognition

    Cell · 1994 · 10.1016/0092-8674(94)90292-5

  • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA

    Journal of Molecular Biology · 1991 · 10.1016/0022-2836(91)90754-t

  • Protein Hydration in Aqueous Solution

    Science · 1991 · https://doi.org/10.1126/science.1948083

  • NMR with Proteins and Nucleic Acids

    Europhysics news · 1986 · https://doi.org/10.1051/epn/19861701011

  • Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry

    Journal of Molecular Biology · 1985 · 10.1016/0022-2836(85)90347-x

  • Calibration of the angular dependence of the amide proton-Cα proton coupling constants, 3JHNα, in a globular protein

    Journal of Molecular Biology · 1984 · 10.1016/0022-2836(84)90035-4

  • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances

    Journal of Molecular Biology · 1984 · 10.1016/0022-2836(84)90034-2

  • Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filtering

    Biochemical and Biophysical Research Communications · 1983 · 10.1016/0006-291x(83)91225-1

  • Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

    Journal of Molecular Biology · 1983 · 10.1016/s0022-2836(83)80144-2

  • Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins

    Biochemical and Biophysical Research Communications · 1983 · 10.1016/0006-291x(83)91093-8

  • Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra

    Journal of Molecular Biology · 1982 · 10.1016/0022-2836(82)90008-0

  • Experimental techniques of two-dimensional correlated spectroscopy

    Journal of Magnetic Resonance (1969) · 1980 · 10.1016/0022-2364(80)90255-3

  • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

    Biochemical and Biophysical Research Communications · 1980 · 10.1016/0006-291x(80)90695-6

  • 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐ L ‐Ala‐OH

    Biopolymers · 1979 · 10.1002/bip.1979.360180206

Current projects

    No projects listed.