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DESCRIPTION (provided by applicant): In this proposal, funds are requested to acquire a 500 MHz NMR spectrometer to support biomedical research at Weill Medical College of Cornell University. The instrument will directly support 16 NIH funded research grants and serve as a core resource for the medical college. Currently, the university has one NMR spectrometer dedicated for NMR structural analysis of proteins. There is a growing need at Weill-Cornell for analysis of synthetic compounds, natural products and small peptides for a variety of biological and medicinal studies. The requested instrument will significantly reduce the burden on the sole spectrometer, provide analytical capability for biological and synthetic chemistry, and support the newly established Chemical Synthesis Core facility. The NMR spectrometer will be optimized for both small molecule and peptide studies. The NMR will include an inverse 1H/13C/15N probe with three radio frequency channels enabling triple resonance experiments. The instrument will have capabilities that do not currently exist at Weill-Cornell and are unavailable locally. These include: 1) a broad-band probe for direct detection of 1H, 19F, 31P, 11B, 13C, 23Na, and 15N; 2) a multi-sampler for automated sample insertion and data acquisition; and 3) an expanded temperature range for data collection from -150 ¿C to 180 ¿C. The instrument will be located in the NMR Core facility, the only source of analytical NMR available to researchers at Weill Medical College of Cornell University. Relevance: NMR spectrometers are essential for molecular structure determination and chemical identification. The acquisition of a 500 MHz NMR will directly support NIH sponsored research aimed at understanding and combating bacterial infection, malaria, AIDS, cancer, tuberculosis, Alzheimer's, Parkinson's and cardiovascular diseases. The instrument purchased will be employed to identify and characterize proteins and peptides involved in disease processes that might serve as pharmaceutical targets, as well as synthetic molecules that influence bioactivity.
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NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state.
尿素变性状态下 BDNF 前结构域变体的 NMR 主链共振分配。
DOI: 10.1007/s12104-017-9777-0
发表时间: 2018
期刊: Biomolecular NMR assignments
影响因子: 0.9
作者: [Wang,Jing, Bains,Henrietta, Anastasia,Agustin, Bracken,Clay]
通讯作者: Bracken,Clay
Structure and Interactions of BDNF
Acquisition of a Cold Probe and Console for a 600MHz NMR spectrometer
NMR STUDIES OF THE C-TERMINAL DOMAIN OF TENASCIN
NMR STUDIES OF THE C-TERMINAL DOMAIN OF TENASCIN