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BSI Proteomics Introduces New Service-Structure Activity Relationships (SAR) by Nuclear Magnetic Resonance

Gaithersburg, Md., May 2, 2005- BSI Proteomics Corporation, a privately held CRO, has launched a new service utilizing NMR spectroscopy techniques such as Saturation Transfer Detection (STD) and Water-LOGSY to study receptor-ligand interactions.  Recent advances in genomic sequencing and bioinformatic methods for gene annotation have provided a wealth of new potential drug targets for the treatment of infectious, degenerative and chronic diseases. NMR spectroscopy is a unique tool due to its versatility and high-throughput capabilities, together with the ability of the technology to provide atomic level information on very large compound sets and their complexes with drug targets. These techniques show advantages over traditional diffusion based methods, most notably in their overall sample and concentration requirements.  NMR is uniquely powerful in the early phases of drug discovery, because it allows screening over a wide range of affinities (mM-nM) and allows a quantitative description and characterization of dynamic processes at the binding site of a target molecule, which can be crucial to understand the details of drug-receptor interactions.  BSI Proteomics has open access to high field NMR spectrometers equipped with cryoprobes.  

BSI Proteomics Corporation is a privately held Platform Technology company.  The company provides total contract research services from protein expression to structure determination and ligand screening.  BSI offers leasing plans for its Platform Technologies, and develops proprietary proteins for licensing purposes.  BSI scientists have integrated and utilized their flagship technology, the Automated Robotic Dynamic Crystallization System™ (ARD™) to crystallize soluble, membrane and ion channel proteins in many different dynamically controlled conditions, simultaneously. The company actively partners with pharmaceutical and biotechnology companies, associations and universities to provide rational, structure-based approaches for the discovery of new drugs with the utilization of Dynamic Crystallization Platform Technologies.  

For further information please contact

Dr. Soojay Banerjee (E-mail: soojay@bsiproteomics.com)

Ph: 301-990-3586

101 Lakeforest Blvd. Suite 300

Gaithersburg, MD 20877

www.bsiproteomics.com

 


 

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