CRYOPROBE ACCESSORY FOR A 600 MHZ NMR SPECTROMETER: B ANTHRACIS

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This subproject is one of many research subprojects utilizing the resources provided by a Shared Instrumentation 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 grant, which is not necessarily the institution for the investigator. DESCRIPTION (provided by applicant): The 600 MHz NMR Spectrometer (Bruker Avance-600) at the NMR Shared Facility of the University of Alabama at Birmingham currently provides the highest operating field available for the faculty members on the campus. It is being utilized by a diverse group of investigators working on projects ranging from the characterization of trace amounts of compounds requiring high sensitivity detection to the three dimensional structure determinations of proteins by 3D/4D-NMR spectroscopy. To significantly enhance the efficiency of this instrument in accommodating these research projects on biomolecular systems, a request is made for the purchase of a triple resonance inverse CryoProbe accessory for the 600 MHz NMR system. This probe provides a sensitivity enhancement of 300% to 400% (depending upon the sample) over the conventional room temperature probe, and will dramatically and significantly enhance the capabilities of the 600 MHz NMR spectrometer in meeting the needs of the UAB campus. With the significant improvement in sensitivity, the instrument can :(i) reduce data acquisition times for 3D/4D-NMR measurements on isotopically labeled proteins from several weeks or months to just a few days, (ii) increase the through-put of NMR samples, (iii) permit the study of biomolecules that are available only in low concentrations or only sparingly soluble, (iv) permit the structural study of proteins and compounds that have a limited life time, and (v) permit the structural characterization of proteins that tend to dimerize at mM concentrations but are predominantly monomeric at low concentrations. This 600 MHz CryoProbe upgrade will have a significant impact upon the programs of a major user group consisting of eight faculty members with research projects dealing with multidimensional NMR structural investigations on human apolipoprotein A-l, interferon-tau, cardiac muscle regulatory proteins, interaction of calmodulin with HIV gp41, bacteriophage P22 scaffolding protein, drug/DNA complexes, surface oligosaccahrides isolated from the Bacillus anthracis Exosporium, and the 1H and ISC-characterization of metabolic intermediates in low concentration.