Kurt Wüthrich
Researcher Next ID · RN-021249
Researcher · Biochemistry, Genetics and Molecular Biology
San Diego, Switzerland
- Works count
- 1,000
- Citation count
- 99,120
- H-index
- 144
- i10-index
- 597
Research interests
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
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