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      Kurt Wüthrich

      Kurt Wüthrich

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      Human Institute, ShanghaiTech University, Shanghai 201210, China | Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093 Zürich, Switzerland | ...

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      Kurt Wüthrich:Expert Impact

      Concepts for whichKurt Wüthrichhas direct influence:Nmr structure,Magnetic resonance,Solution structure,Nuclear magnetic resonance,Nuclear magnetic,Aqueous solution,Spectroscopy models,Resonance spectroscopy.

      Kurt Wüthrich:KOL impact

      Concepts related to the work of other authors for whichfor which Kurt Wüthrich has influence:Solution structure,Magnetic resonance,Prion protein,Amino acid,Nmr spectroscopy,Escherichia coli,Models molecular.

      KOL Resume for Kurt Wüthrich

      Year
      2022

      Human Institute, ShanghaiTech University, Shanghai 201210, China

      Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093 Zürich, Switzerland

      Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA 92037, USA

      2021

      Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA, USA

      iHuman Institute, ShanghaiTech University, China

      2020

      Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

      Human Institute, ShanghaiTech University, Shanghai 201210, China;, (J.Z.);, (W.Y.);, (W.D.);, (K.W.)

      Institute for Molecular Biology and Biophysics, ETH Zürich, Zürich, Switzerland

      2019

      School of Life Science and Technology, ShanghaiTech University, 393 Hua Xia Zhong Road, 201210, Pudong, Shanghai, China

      Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, 92037, La Jolla, CA, USA

      2018

      Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California, 92037, United States

      Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, CA, USA

      2017

      Department of Integrative Structural and Computational Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, United States of America

      iHuman Institute, ShanghaiTech University, 393 Middle Huaxia Road, 201210, Shanghai, China

      Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, CH-8093 Zurich, Switzerland;

      2016

      Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA

      iHuman Institute, ShanghaiTech University, 99 HaiKe Road, 201210, Shanghai, China

      ETH Zurich Institute of Molecular Biology and Biophysics Zurich Switzerland

      Joint Center for Structural Genomics, http://www.jcsg.org

      The Scripps Research Institute Department of Integrative Structural and Computational Biology La Jolla California

      2015

      The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037

      Department of Molecular Biology and Biophysics, ETH Zurich, CH-8093 Zurich, Switzerland;

      GPCR‐Network, 3430 S. Vermont Ave., TRF 105, Los Angeles, CA 90089‐3301 (USA), Fax: (+1) 858‐784‐8014 http://gpcr.usc.edu

      Institute of Molecular Biology and Biophysics, ETH Zurich, Otto‐Stern‐Weg 5, 8093 Zurich (Switzerland)

      2014

      Institut für Molekularbiologie und Biophysik, ETH Zürich, CH-8093 Zürich, Switzerland,

      Joint Center for Structural Genomics, 92037, La Jolla, CA, USA

      Department of Integrated Structural and Computational Biology, The Scripps Research Institue, La Jolla, CA 92037

      2013

      Joint Center for Structural Genomics and Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA, USA

      The Scripps Research Institute Department of Integrative Structural and Computational Biology La Jolla CA

      Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zürich, CH-8093 Zurich, Switzerland;

      Department of Integrative Structural and Computational Biology and

      2012

      Institute of Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland

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      Sample of concepts for which Kurt Wüthrich is among the top experts in the world.
      Concept World rank
      solventexposed clusters #1
      f175 y169 #1
      np2472991 #1
      manyparameter characterization #1
      distance geometry program #1
      prokaryotic repressors #1
      conformational space conformers #1
      membrane protein ompx #1
      polar protozoan ciliate #1
      proteins nmr #1
      structure determination input #1
      diastereotopic substituents #1
      cis conformations species #1
      current calculations #1
      homologous pheromones #1
      octamer repeat ocre #1
      noes protein protons #1
      backbone protons total #1
      seminal inhibitor #1
      4fphe glucagon #1
      hz 15n #1
      kurt wüthrich #1
      new software candid #1
      differences solution structure #1
      macromolecules exchange #1
      correct fold cycle #1
      kinase isoenzymes coli #1
      murine prp nmr #1
      xenopus laevis xlprp #1
      xlprp globular domain #1
      groel cypa #1
      reporter residues #1
      protein targets proteins #1
      mnk3 #1
      500 mhz assignments #1
      nmr probes #1
      local differences structures #1
      micelle surface #1
      165–171 #1
      solution trosy #1
      nuclear magnetic resonance #1
      omps nmr #1
      fimf #1
      griffey #1
      diana spectroscopy models #1
      cys11pro12tyr13cys14 #1
      proteins exchange rates #1
      residues intact pdomain #1
      program mapper #1
      regular helix #1
      Sign-in to see all concepts, it's free!

      Prominent publications by Kurt Wüthrich

      KOL-Index: 14318

      Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all ...

      Known for Protein Nmr | New Software | Automated Assignment | Torsion Angle Dynamics | Structure Determination
      KOL-Index: 13948

      The determination of the NMR structure of oxidized Escherichia coli glutaredoxin in aqueous solution is described, and comparisons of this structure with that of reduced E. coli glutaredoxin and the related proteins E. coli thioredoxin and T4 glutaredoxin are presented. Based on nearly complete sequence-specific 1H-NMR assignments, 804 nuclear Overhauser enhancement distance constraints and 74 dihedral angle constraints were obtained as the input for the structure calculations, for which ...

      Known for Coli Glutaredoxin | Nmr Structure | Active Site | Thioredoxin Proteins | Spectroscopy Models
      KOL-Index: 12815

      DnaJ from Escherichia coli is a 376-amino acid protein that functions in conjunction with DnaK and GrpE as a chaperone machine. The N-terminal fragment of residues 2-108, DnaJ-(2-108), retains many of the activities of the full-length protein and contains a structural motif, the J domain of residues 2-72, which is highly conserved in a superfamily of proteins. In this paper, NMR spectroscopy was used to determine the secondary structure and the three-dimensional polypeptide backbone fold ...

      Known for Escherichia Coli | Secondary Structure | Highly Conserved | Dnaj Molecular Chaperone | Nmr Spectroscopy
      KOL-Index: 12337

      A novel procedure for efficient computation of three-dimensional protein structures from nuclear magnetic resonance (n.m.r.) data in solution is described, which is based on using the program DIANA in combination with the supporting programs CALIBA, HABAS and GLOMSA. The first part of this paper describes the new programs DIANA. CALIBA and GLOMSA. DIANA is a new, fully vectorized implementation of the variable target function algorithm for the computation of protein structures from ...

      Known for Program Diana | Protein Structures | Nuclear Magnetic | Resonance Data | Efficient Computation
      KOL-Index: 12317

      Membrane proteins are usually solubilized in polar solvents by incorporation into micelles. Even for small membrane proteins these mixed micelles have rather large molecular masses, typically beyond 50000 Da. The NMR technique TROSY (transverse relaxation-optimized spectroscopy) has been developed for studies of structures of this size in solution. In this paper, strategies for the use of TROSY-based NMR experiments with membrane proteins are discussed and illustrated with results ...

      Known for Membrane Proteins | Escherichia Coli | Nmr Studies | Mixed Micelles | Ompx Dhpc
      KOL-Index: 11917

      The spin labels, 5-doxylstearate, 12-doxylstearate, 16-doxylstearate and 1-oxyl-2,2,6,6-tetramethyl-4-dodecylphosphopiperidine, have been incorporated into dodecylphosphocholine micelles and mixed dodecylphosphocholine glucagon micelles. The EPR spectral parameters for the different spin labels and the 1H- and 13C-NMR relaxation rates for nuclei of the detergent molecules indicated that inclusion of up to one spin label molecule per micelle had little influence on the spatial ...

      Known for Micelle Surface | Spin Labels | Resonance Spectroscopy | Nmr Studies | Polypeptide Chain
      KOL-Index: 11642

      The DNA-binding domain of the phage 434 repressor consisting of N-terminal residues 1 to 69 (434 repressor(1-69)), was expressed in Escherichia coli with natural isotope abundance, uniform 15N-labeling and biosynthetically directed fractional 13C-labeling in extent of about 10%. With these protein preparations the three-dimensional structure was determined in solution. The techniques used were nuclear magnetic resonance (n.m.r.) spectroscopy for the collection of conformational ...

      Known for 434 Repressor | Solution Structure | Magnetic Resonance | Binding Domain | Residues 1
      KOL-Index: 11639

      Novel algorithms are presented for automated NOESY peak picking and NOE signal identification in homonuclear 2D and heteronuclear-resolved 3D [1H,1H]-NOESY spectra during de novoprotein structure determination by NMR, which have been implemented in the new software ATNOS (automated NOESY peak picking). The input for ATNOS consists of the amino acid sequence of the protein, chemical shift lists from the sequence-specific resonance assignment, and one or several 2D or 3D NOESY spectra. In ...

      Known for Noesy Spectra | Protein Nmr | Structure Determination | Automated Assignment | Signal Identification
      KOL-Index: 11582

      A novel approach for studies of amide proton exchange in proteins is presented. It relies on measurements of the amide proton-Cα proton cross-peak intensities in the two-dimensional homonuclear correlated 1H nuclear magnetic resonance spectra. The protein is dissolved in 2H2O and the solution is exposed to the conditions of p2H and temperature where the exchange rates are to be measured. After variable intervals, the amide proton exchange in a sample of this protein solution is quenched ...

      Known for Proton Exchange | Magnetic Resonance | Pancreatic Trypsin | Dimensional Nuclear | Protein Surface
      KOL-Index: 11575

      Fast transverse relaxation of 1H, 15N, and 13C by dipole-dipole coupling (DD) and chemical shift anisotropy (CSA) modulated by rotational molecular motions has a dominant impact on the size limit for biomacromolecular structures that can be studied by NMR spectroscopy in solution. Transverse relaxation-optimized spectroscopy (TROSY) is an approach for suppression of transverse relaxation in multidimensional NMR experiments, which is based on constructive use of interference between DD ...

      Known for Nmr Structures | Chemical Shift | Dipole Coupling | 15n Relaxation | 750 Mhz
      KOL-Index: 11554

      A previously characterized modification of the basic pancreatic trypsin inhibitor (BPTI), with the carbonyl carbon atom of Lys-15 selectively enriched in 13C, the peptide bond Arg-39--Ala-40 cleaved, and Arg-39 removed, was used for 13C NMR studies of the reactive site peptide bond Lys-15--Ala-16 in the complexes with trypsin, trypsinogen, and anhydrotrypsin. The chemical shift of [1-13C]Lys-15 was 175.7 ppm in the free inhibitor, 176.4 ppm in the complexes with trypsin and ...

      Known for Trypsin Inhibitor | Reactive Site | Peptide Bond | Magnetic Resonance | Chemical Shift

      Key People For Nmr Structure

      Top KOLs in the world
      #1
      Kurt Wüthrich
      nmr structure magnetic resonance aqueous solution
      #2
      Adriaan Bax
      dipolar couplings solution structure chemical shift
      #3
      G Marius Clore
      solution structure magnetic resonance spectroscopy models
      #4
      Martin A Billeter
      measles virus viral rna nmr structure
      #5
      Frank Delaglio
      dipolar couplings principal component analysis protein therapeutics
      #6
      Peter Güntert
      solution structure nmr spectra magnetic resonance

      Human Institute, ShanghaiTech University, Shanghai 201210, China | Institute of Molecular Biology and Biophysics, ETH Zürich, Otto-Stern-Weg 5, 8093 Zürich, Switzerland | Department of Integrative Structural and Computational Biology, Scripps Researc

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