Nicholas Ronald Wurtz - Pennington NJ, US Eldon Scott Priestley - Yardley PA, US Daniel L. Cheney - Ringoes NJ, US Peter W. Glunz - Yardley PA, US Xiaojun Zhang - Furlong PA, US Brandon Parkhurst - Twin Rivers NJ, US Vladimir Ladziata - Ewing NJ, US Luciano Mueller - Princeton NJ, US
Keith Lewis Constantine - Langhorne PA, US Brian Lee Claus - Lambertville NJ, US Malcolm Evan Davis - Lambertville NJ, US William Joseph Metzler - Doylestown PA, US Luciano Mueller - Princeton NJ, US
Assignee:
Bristol-Myers Squibb Company - Princeton NJ
International Classification:
G06F 19/00 G01N 33/50 G06G 7/48
US Classification:
702 20, 702 19, 703 11
Abstract:
A method of enhancing the throughput and applicability of NMR-based structure determination of protein-ligand complexes is disclosed. The method circumvents the need for protein sequence-specific resonance assignments and combines NMR data analysis and ligand docking methods into an integrated process. In one embodiment, NMR data is used to filter docking results to identify the most consistent binding modes, thereby providing structural information in a high-throughput fashion without the need for assigning protein resonances. Trial assignments for protein-ligand nuclear Overhauser effect (NOE) interactions are also produced by the method.
Nuclear Magnetic Resonance Method For Identifying Ligands To Target Compounds
Keith Lewis Constantine - Langhorne PA, US Brian Lee Claus - Lambertville NJ, US Malcolm Evan Davis - Lambertville NJ, US William Joseph Metzler - Doylestown PA, US Luciano Mueller - Princeton NJ, US
Assignee:
Bristol-Myers Squibb Company - Princeton NJ
International Classification:
G06F 19/00 G01N 33/48 G06G 7/48
US Classification:
702 20, 702 19, 703 11
Abstract:
A method of enhancing the throughput and applicability of NMR-based structure determination of protein-ligand complexes is disclosed. The method circumvents the need for protein sequence-specific resonance assignments and combines NMR data analysis and ligand docking methods into an integrated process. In one embodiment, NMR data is used to filter docking results to identify the most consistent binding modes, thereby providing structural information in a high-throughput fashion without the need for assigning protein resonances. Trial assignments for protein-ligand nuclear Overhauser effect (NOE) interactions are also produced by the method.
- Princeton NJ, US Haiying Tang - Morganville NJ, US Paul E Morin - Pennington NJ, US Harold J. Malone - Spring Lake NJ, US Luciano MUELLER - Princeton NJ, US
International Classification:
A61K 49/18 A61K 47/68 A61K 49/12
Abstract:
Deuterated polymer-biomolecule conjugates and the synthesis and use of deuterated polymer-biomolecule conjugates for detecting the location of specific molecules, e.g., cell surface molecules, in a subject, and for imaging various processes within the body, for detecting the location of molecules associated with disease pathology, and for monitoring disease progression are disclosed.
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