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.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR021064-01A1
Application #
7335033
Study Section
Special Emphasis Panel (ZRG1-BCMB-Q (30))
Project Start
2006-05-15
Project End
2007-05-14
Budget Start
2006-05-15
Budget End
2007-05-14
Support Year
1
Fiscal Year
2006
Total Cost
$40,125
Indirect Cost
Name
University of Alabama Birmingham
Department
Biochemistry
Type
Schools of Medicine
DUNS #
063690705
City
Birmingham
State
AL
Country
United States
Zip Code
35294
Shin, Ronald; Tzou, Ywh-Min; Wong, Hing C et al. (2012) 1H, 15N, and 13C resonance assignments for a monomeric mutant of the HIV-1 capsid protein. Biomol NMR Assign 6:131-4
Shin, Ronald; Tzou, Ywh-Min; Krishna, N Rama (2011) Structure of a monomeric mutant of the HIV-1 capsid protein. Biochemistry 50:9457-67
Mishra, Vinod K; Palgunachari, Mayakonda N; Hudson, Jason S et al. (2011) Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR. Biochim Biophys Acta 1808:498-507
Lu, Shi-En; Novak, Jan; Austin, Frank W et al. (2009) Occidiofungin, a unique antifungal glycopeptide produced by a strain of Burkholderia contaminans. Biochemistry 48:8312-21
Shin, Ronald; Welch, Danny R; Mishra, Vinod K et al. (2009) Nuclear magnetic resonance and circular dichroism study of metastin (Kisspeptin-54) structure in solution. Clin Exp Metastasis 26:527-33
Mishra, Vinod K; Palgunachari, Mayakonda N; Krishna, Rama et al. (2008) Effect of leucine to phenylalanine substitution on the nonpolar face of a class A amphipathic helical peptide on its interaction with lipid: high resolution solution NMR studies of 4F-dimyristoylphosphatidylcholine discoidal complex. J Biol Chem 283:34393-402