• Publications
  • Influence
NMR of proteins and nucleic acids
Introduction and Survey. THE FOUNDATIONS: STRUCTURE AND NMR OF BIOPOLYMERS. NMR of Amino Acid Residues and Mononucleotides. NMR Spectra of Proteins and Nucleic Acids in Solution. The NMR AssignmentExpand
MOLMOL: a program for display and analysis of macromolecular structures.
Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, and identification and listing of short distances between pairs of hydrogen atoms. Expand
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. Expand
Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.
The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins and shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDIDs approach results in greatly enhanced efficiency of the NOESY spectral analysis. Expand
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.
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. Expand
A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules.
The 2D NOE experiment has the principal advantage that it avoids detrimental effects arising from the limited selectivity of preirradiation in crowded spectral regions, and yields with a single instrument setting a complete network of NOE's between all the protons in the macromolecule. Expand
Improved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filtering.
The elimination of the dispersive character of the diagonal peaks in phase-sensitive, double quantum-filtered COSY spectra allows identification of cross peaks lying immediately adjacent to the diagonal, which represents a significant improvement over the conventional COSy experiment. Expand
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
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. Expand
NMR solution structure of the human prion protein.
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. Expand
An EB1-Binding Motif Acts as a Microtubule Tip Localization Signal
Structural and biochemical data reveal the molecular basis of the EB1-SxIP interaction and explain its negative regulation by phosphorylation and establish a general "microtubule tip localization signal" (MtLS) and delineate a unifying mechanism for this subcellular protein targeting process. Expand