W
Werner Klaus
Researcher at Hoffmann-La Roche
Publications - 11
Citations - 760
Werner Klaus is an academic researcher from Hoffmann-La Roche. The author has contributed to research in topics: Protein secondary structure & Nuclear magnetic resonance spectroscopy. The author has an hindex of 8, co-authored 11 publications receiving 740 citations.
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Journal ArticleDOI
Novel inhibitors of DNA gyrase: 3D structure based biased needle screening, hit validation by biophysical methods, and 3D guided optimization. A promising alternative to random screening.
Hans-Joachim Boehm,Markus Boehringer,Daniel Bur,Hans Gmuender,Walter Huber,Werner Klaus,Dirk Kostrewa,Holger Kuehne,Thomas Luebbers,Nathalie Meunier-Keller,Francis Mueller +10 more
TL;DR: This work combines as key techniques an in silico screening for potential low molecular weight inhibitors, a biased high throughput DNA gyrase screen, validation of the screening hits by biophysical methods, and a 3D guided optimization process.
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Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution.
TL;DR: The covalent and non-covalent interaction sites are clearly separated on the HsUbc2b surface, while no such clear-cut segregation of the interaction area was observed on ubiquitin.
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The Nuclear Magnetic Resonance Solution Structure of Flavoridin, an Antagonist of the Platelet GP IIb-IIIa Receptor
Hans Senn,Werner Klaus +1 more
TL;DR: The structure of flavoridin consists essentially of non-repetitive elements such as tight turns and loops, whose location and conformation are characterized in this paper.
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Determination of the Disulphide Bonding Pattern in Proteins by Local and Global Analysis of Nuclear Magnetic Resonance Data: Application to Flavoridin
TL;DR: The use of both local and global proton-proton nuclear Overhauser enhancement (NOE) distance information for the identification of the disulphide bridge network in cysteine-rich polypeptides was investigated by statistical analysis of the crystal structures of a selected group of proteins.
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Determination of the solution structure of the SH3 domain of human p56 Lck tyrosine kinase.
TL;DR: The solution structure of the SH3 domain of human p56 Lck tyrosine kinase (Lck-SH3) has been determined by multidimensional heteronuclear NMR spectroscopy by exploiting the stereo-specific assignment of prochiral methyl groups.