Brian Lee Claus

US Patent:

8504304, Aug 6, 2013

Filed:

Feb 3, 2012

Appl. No.:

13/365347

Inventors:

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.

US Patent:

8150634, Apr 3, 2012

Filed:

Nov 10, 2005

Appl. No.:

11/272262

Inventors:

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.