This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The Hunt lab has collected data at NECAT for three different NIH-funded projects: 1. NIH/GM (1R01GM072867-01) PI: J.F. Hunt August 2005 ?July 2009 Structural mechanics of MsbA-family ABC Transporters. The objectives of this application are to perform crystal structure determinations of a model ABC Transporter integral membrane protein complex in various nucleotide-bound and ligand-bound states in order to develop and complete structural and thermodynamic understanding of transport mechanism. 2. NIH/GM (U54GM074958-01) PI: G.T. Montelione July2005 ?June 2010 Structural genomics of eukaryotic model organisms. This center grant supports the continuation of the Northeast Structural Genomics Consortium (NESG), a collaboration between 17 laboratories from 8 institutions. The primary goal of this project is to develop integrated technologies for high-throughput protein production and 3D structure determination while producing approximately 200 new protein structures per year. Dr. Hunt's role in this project comprises development and supervision of the high-throughput protein crystallization lab, currently producing about 60 new proteins crystal structures per year and expected to produce approximately 120 per year by the conclusion of the new award period. 3. NIH/GM (R01GM077360-01) PI: J.F. Hunt December 2007 ?November 2011 Structure, mechanism, and inhibition of AlkB homologues. The objectives of this grant are to perform joint structural, enzymological, and QM/MM computational studies of the mechanism of oxidative DNA repair by E. coli AlkB, to determine crystal structures for some of the 8 homologous enzymes in humans, and to identify and characterize high affinity inhibitors of these latter enzymes. Richard Friesner of the Columbia Chemistry Department is a co-PI on the QM/MM (quantum mechanics / molecular mechanics) studies and use of virtual screening for inhibitor identification.
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