Acquisition of a 700 MHz NMR Spectrometer

购买 700 MHz NMR 波谱仪

• 批准号: 8734882
• 负责人: ELISAR J BARBAR
• 金额: $ 130万
• 依托单位: OREGON STATE UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2015
• 资助国家: 美国
• 起止时间: 2015-02-27 至 2017-02-26
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8734882
• 关键词: Aging; Biological Factors; Biomedical Research; Biomolecular Nuclear Magnetic Resonance; Catalysis; Cataract; Disease; Dynein ATPase; Ensure; Environment; Enzymes; Fostering; Funding; Growth; HIV; Health Sciences; Housing; Institution; Lead; Maintenance; Molecular Structure; Motor; Nuclear Magnetic Resonance; Oregon; Productivity; Protein Dynamics; Proteins; Research; Research Infrastructure; Research Personnel; Research Support; Role; Sampling; Science; Solubility; Solutions; Students; United States National Institutes of Health; Universities; base; cost; deamidation; instrument; instrumentation; interest; macromolecular assembly; meetings; protein complex; small molecule

This request is for funds to acquire a 4-channel 700 MHz nuclear magnetic resonance (NMR) spectrometer for solution studies of macromolecular structures and assemblies. The instrument will be equipped with a high-sensitivity triple resonance (1H, 13C, 15N) TCI cryoprobe that will substantially enhance sensitivity and permit analysis of samples with limited solubility. There is currently no high field instrument dedicated for macromolecular NMR at Oregon State University. The macromolecular NMR group previously utilized a Bruker DRX 600 MHz instrument that was purchased in 1994 but has been non-functional and mothballed since February 2012. The new instrument is critical for the needs of several NIH-supported Oregon State University researchers and other biomedical researchers from Oregon Health Science University, University of Oregon, Portland State University and smaller institutions in the region. Proposed major studies include the role of natively disordered proteins in macromolecular assembly, particularly in the dynein motor protein complex, protein deamidation in cataractous lens and aging, the role of protein dynamics in enzyme catalysis and mechanistic studies on various diseases including HIV and ALS. Continued productivity and growth to meet the needs of the existing NMR group and the expanding user base depend on this acquisition. The new instrument will be housed in the recently renovated space in the campus-wide NMR facility that is presently equipped with instrumentation dedicated to natural products and small organic molecules. Its incorporation into a pre-existing NMR center will ensure optimal maintenance and usage of this cutting-edge instrument. Oregon State University is committed to building a strong campus-wide NMR core that unites small molecule and biomolecular NMR facilities, and is supporting this proposal with a substantial match towards the cost of the instrument and recurring support towards operating costs to help build the user base and ensure the instrument is widely accessible even to students with limited access to funding. Dr. Barbar's protein NMR expertise and track record in acquiring multi-user instruments and interest in promoting a widely accessible facility enabling significant, biomedically relevant research make her uniquely suited to lead this effort. This purchase will be the first of its kind on campus and will have an immediate impact on the infrastructure at Oregon State University and participating institutions as it will enable cutting-edge science, foster highly collaborative biomedical research, and support the vibrant research environment in the State of Oregon.

这项请求是为购买一台4通道700兆赫核磁共振（NMR）光谱仪提供资金

项目成果

Untargeted Identification of Alkyne-Containing Natural Products Using Ruthenium-Catalyzed Azide Alkyne Cycloaddition Reactions Coupled to LC-MS/MS.

• DOI: 10.1021/acs.jnatprod.1c00798
• 发表时间: 2022-01-28
• 期刊: Journal of natural products
• 影响因子: 5.1
• 作者: Back D;Shaffer BT;Loper JE;Philmus B
• 通讯作者: Philmus B

Structural characterization of the self-association domain of swallow.

燕子自关联域的结构表征。

• DOI: 10.1002/pro.4055
• 发表时间: 2021
• 期刊: Protein science : a publication of the Protein Society
• 作者: Loening,NikolausM;Barbar,Elisar
• 通讯作者: Barbar,Elisar

The LC8 Recognition Motif Preferentially Samples Polyproline II Structure in Its Free State.

LC8 识别基序优先采样游离态的聚脯氨酸 II 结构。

• DOI: 10.1021/acs.biochem.7b00552
• 发表时间: 2017
• 期刊: Biochemistry
• 影响因子: 2.9
• 作者: Morgan,JessicaL;Jensen,MaleneRingkjøbing;Ozenne,Valéry;Blackledge,Martin;Barbar,Elisar
• 通讯作者: Barbar,Elisar

Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes

• DOI: 10.1016/j.bpj.2020.07.023
• 发表时间: 2020-09-01
• 期刊: BIOPHYSICAL JOURNAL
• 影响因子: 3.4
• 作者: Loening, Nikolaus M.;Saravanan, Sanjana;Barbar, Elisar
• 通讯作者: Barbar, Elisar

RNA structure and multiple weak interactions balance the interplay between RNA binding and phase separation of SARS-CoV-2 nucleocapsid.

• DOI: 10.1093/pnasnexus/pgad333
• 发表时间: 2023-10
• 期刊: PNAS NEXUS
• 作者: Estelle, Aidan B.;Forsythe, Heather M.;Yu, Zhen;Hughes, Kaitlyn;Lasher, Brittany;Allen, Patrick;Reardon, Patrick N.;Hendrix, David A.;Barbar, Elisar J.
• 通讯作者: Barbar, Elisar J.