Research in this laboratory is centered around solution studies on the structure and dynamics of proteins, protein-protein complexes and protein-nucleic acid complexes using multidimensional NMR spectroscopy, and on the development and application of novel NMR and computational methods to aid in these studies. Over the last year we have developed several new multidimensional pulse sequences to derive assignments using direct-carbon detect methods;multidimensional sequences to detect arginine guanidino and lysine NH3 groups;new approaches to docking protein-protein complexes based on very sparse intermolecular NOE data;various computational approaches to facilitate structure determination and automation;and we have solved the structures of several large protein-protein complexes, including a phosphoryl transfer complexes of enzymes IIAMannitol and IIBMannitol, IIAmannose and IIBMannose, IIAChitobiose-IIBChitobiose from the bacterial phosphoryl transfer system. In addition, we have devoted significant efforts towards detecting, characterizing and visualizing highly transient, lowly-populated states that are invisible to conventional biophysical and structural techniques, yet play a key role in numerous biological processes including recognition, allostery, signal transduction, etc.... by means of paramagnetic relaxation enhancement (PRE) methods. Using this approach we have been able to characterize the initial stages invlved in autoprocessing of HIV-1 protease.
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