The New York Structural Biology Center, a 501(c) (3) corporation governed by a Board representing nine research institutions, proposes to purchase a 900 MHz NMR spectrometer for research in structural biology, and seeks fluids for art of the Cost of the spectrometer. The principal investigators and other investigators will share in the use of this resource, and will encourage other users. Research to be constructed includes structure determination of proteins and nucleic acids, dynamics studies, protein folding, and development of methods of isotopic labeling, application to higher molecular weights, and application to membrane proteins. These studies are part of programs aimed at understanding both basic scientific problems in structural biology and at physiological and pathological processes involved in many diseases of development, cancer, muscle skeletal disorders, neurological diseases, and infectious diseases. The investigators include leading structural biologists using NMR, and leading experimentalists and methods developers in the area. This rich intellectual environment will be fruitful for scientific productivity, creativity, and collaboration using the proposed instrument. The 900 MHz spectrometer will be housed in a 10,000 sq. if. extension now in construction, contiguous with the NYSBC's existing laboratory. The investigators will have access to' 800 MHz and lower field instruments, so that the 900 MHz system Can be used selectively for those experimentalists requiring ultra high field. Specific requirement S for ultra high field include applications to large molecular weight systems using transverse optimize relaxation spectroscopy (TROSY) and its ''derivatives, magnetic orientation for measurement of residual dipolar couplings, and field-dependent CSA, dynamics, and other relaxation-related phenomena.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Biotechnology Resource Grants (P41)
Project #
5P41GM066354-02
Application #
6605633
Study Section
Special Emphasis Panel (ZRG1-BNP (01))
Program Officer
Wehrle, Janna P
Project Start
2002-07-01
Project End
2007-06-30
Budget Start
2003-07-01
Budget End
2004-06-30
Support Year
2
Fiscal Year
2003
Total Cost
$350,200
Indirect Cost
Name
New York Structural Biology Center
Department
Type
DUNS #
011191520
City
New York
State
NY
Country
United States
Zip Code
10027
Hsu, Andrew; O'Brien, Paul A; Bhattacharya, Shibani et al. (2018) Enhanced spectral density mapping through combined multiple-field deuterium 13CH2D methyl spin relaxation NMR spectroscopy. Methods 138-139:76-84
Vugmeyster, Liliya; Griffin, Aaron; Ostrovsky, Dmitry et al. (2018) Correlated motions of C'-N and C?-C? pairs in protonated and per-deuterated GB3. J Biomol NMR 72:39-54
Wragg, Rachel T; Parisotto, Daniel A; Li, Zhenlong et al. (2017) Evolutionary Divergence of the C-terminal Domain of Complexin Accounts for Functional Disparities between Vertebrate and Invertebrate Complexins. Front Mol Neurosci 10:146
Snead, David; Lai, Alex L; Wragg, Rachel T et al. (2017) Unique Structural Features of Membrane-Bound C-Terminal Domain Motifs Modulate Complexin Inhibitory Function. Front Mol Neurosci 10:154
Dikiy, Igor; Fauvet, Bruno; Jovi?i?, Ana et al. (2016) Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations. ACS Chem Biol 11:2428-37
Huang, Zhifeng; Marsiglia, William M; Basu Roy, Upal et al. (2016) Two FGF Receptor Kinase Molecules Act in Concert to Recruit and Transphosphorylate Phospholipase C?. Mol Cell 61:98-110
Natarajan, Aswin; Nadarajah, Vidushan; Felsovalyi, Klara et al. (2016) Structural Model of the Extracellular Assembly of the TCR-CD3 Complex. Cell Rep 14:2833-45
Athuluri-Divakar, Sai Krishna; Vasquez-Del Carpio, Rodrigo; Dutta, Kaushik et al. (2016) A Small Molecule RAS-Mimetic Disrupts RAS Association with Effector Proteins to Block Signaling. Cell 165:643-55
Gill, Michelle L; Byrd, R Andrew; Palmer III, Arthur G (2016) Dynamics of GCN4 facilitate DNA interaction: a model-free analysis of an intrinsically disordered region. Phys Chem Chem Phys 18:5839-49
Hernández, Griselda; LeMaster, David M (2016) Quantifying protein dynamics in the ps-ns time regime by NMR relaxation. J Biomol NMR 66:163-174

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