In recent years, Nuclear Magnetic Resonance (NMR) spectroscopy has become a powerful tool for studying the three-dimensional structure of proteins in solution. This development was made possible by the introduction of two-dimensional NMR techniques, and has been enhanced by the development of three- and four-dimensional NMR spectroscopy. Today, multidimensional NMR techniques make it possible to determine the structure of proteins up to 50 kDa and protein complexes up to a molecular weight of 65 kDa and more.
Recognition between molecules is a prerequisite in many biological processes such as signal transduction, immune response, enzymatic reactions, translation of the genetic code, protein synthesis and others. Our laboratory uses NMR spectroscopy to study the three-dimensional structure of proteins and protein complexes with their ligands, to understand biological recognition at atomic resolution.
The Weizmann Institute has Bruker 800 MHz and 500 MHz spectrometers both equipped with cryoprobes dedicated almost exclusively to Protein NMR research. Our research is supported by the National Institutes of Health (USA), Minerva (Germany), the US-Israel Binational Science Foundation, Gurwin Foundation and the Kimmelman Center for Macromolecular Structure and Assembly.