✍ Scribed by Steve W. Homans
No coin nor oath required. For personal study only.
Biomolecular NMR spectroscopy has expanded dramatically in recent years and is now a powerful tool for the study of structure, dynamics, and interactions of biomolecules. Previous limitations with respect to molecular size are no longer a primary barrier, and systems as large as 900 kDa were recently studied. NMR spectroscopy is already well‐established as an efficient method for ligand screening. A number of recently developed techniques show promise as aids in structure‐based drug design, for example, in the rapid determination of global protein folds, the structural characterization of ligand–protein complexes, and the derivation of thermodynamic parameters. An advantage of the method is that all these interactions can be studied in solution—time‐consuming crystallization is not necessary. This Review focuses on recent developments in NMR spectroscopy and how they might be of value in removing some of the current “bottlenecks” in structure‐based drug discovery.
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## Abstract The computer program LUDI for automated structure‐based drug design is described. The program constructs possible new ligands for a given protein of known three‐dimensional structure. This novel approach is based upon rules about energetically favourable non‐bonded contact geometries be
## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable v