The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision with which these solution structures can be obtained. Studies aimed at correlating structure and function, and experiments aimed at investigating protein folding are conducted. Structural studies for several proteins have been carried out. These include the DNA binding domains of Mu Transposase and the N-terminal domain of HIV-1 integrase . In addition, work was also carried out on a number of protein nucleic acid complexes, including those of GAGA, Are A and HMG-I/Y. A novel method was developed for large scale preparation of isotopically labelled DNA for structural studies. Also, mutant core libraries of streptococcal Protein G have been prepared and characterized structurally as well as with respect to stability. One of the largest systems whose structure we determined by NMR is the N-terminal domain of Enzyme I of the PTS pathway. In addition, the binding surface for HPr on EI was determined and structural implications of phosphorylation investigated. Finally, the structure of EI-N complexed to HPr was determined
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