Reshma. K*, M.Muthukumaran*, B.krishnamoorthy, Amreen Nishat
Montessori Siva sivani Institute of Science&Technology- College Of
Vijayawada, Andhrapradesh-521 230
Nuclear magnetic resonance (NMR) has progressed rapidly over the last decade as a result of improved experimental technology and development of novel approaches. NMR spectroscopy has evolved into an important technique in support of structure-based drug design. It was most useful as a technique to provide structural information regarding protein drug targets and target–ligand interactions. More recently, it has been shown that NMR may be used as an alternative method for identification of small molecule ligands that bind to protein drug targets. High throughput implementation of these experiments to screen small molecule libraries may lead to identification of potent and novel lead compounds. NMR as a probe of microscopic dynamic behaviour through relaxation and direct diffusion measurements over a wide temperature range is examined.