NMR of proteins and nucleic acids
- K. Wüthrich
- Chemistry, Biology
- 22 March 1988
The NMR Assignment Problem in Biopolymers, two-Dimensional NMR With Proteins and Nucleic Acids, and Sequence-Specific Resonance Assignments.
MOLMOL: a program for display and analysis of macromolecular structures.
Torsion angle dynamics for NMR structure calculation with the new program DYANA.
Test calculations starting from conformers with random torsion angle values showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures.
Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.
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.
- K. Pervushin, R. Riek, G. Wider, K. Wüthrich
- Physics, ChemistryProceedings of the National Academy of Sciences…
- 11 November 1997
The TROSY principle should benefit a variety of multidimensional solution NMR experiments, especially with future use of yet somewhat higher polarizing magnetic fields than are presently available, and thus largely eliminate one of the key factors that limit work with larger molecules.
A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules.
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
- C. Bartels, T. Xia, M. Billeter, P. Güntert, K. Wüthrich
- ChemistryJournal of Biomolecular NMR
- 1 July 1995
XEASY was developed for work with 2D, 3D and 4D NMR data sets to provide maximal computer support for the analysis of spectra, while providing the user with complete control over the final resonance assignments.
Improved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filtering.
NMR solution structure of the human prion protein.
- R. Zahn, A. Liu, K. Wüthrich
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 4 January 2000
The NMR structures of the recombinant human prion protein hPrP(23-230) include a globular domain extending from residues 125-228, for which a detailed structure was obtained, and an N-terminal flexibly disordered "tail," which influences the local conformational state of the polypeptide segments.