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Grant Number: 1C06RR017528-01
PI Name: COWBURN, DAVID A. PI Email: cowburn@nysbc.org PI Title: PRESIDENT & CEO Project Title: EXTRAMURAL RESEARCH FACILITIES CONSTRUCTION Abstract: DESCRIPTION (provided by applicant): The NYSBC, a consortium of nine academic medical research institutions, proposes to construct a 10,000 sq. ft. addition to its existing facilities to house three state-of-the-art cryo EM. The objective is to expand the NYSBC's scientific scope, which currently focuses on magnetic resonance spectroscopy, by creating a resource and program in the complementary field of cryo EM. These new resources will serve a large, internationally-recognized community of National Institutes of Health (NIH)-funded biologists who do not currently have adequate (or any) institutional access to cryo EM. The proposed expansion will serve more than 25 research groups that use cryo EM directly, or in conjunction with crystallography and magnetic resonance spectroscopy, to study proteins and supramolecular machines. Another 40 researchers who do not currently use cryo EM, will be able to undertake more difficult problems in their fields with access to the integrated resources provided by the expanded NYSBC. The NYSBC is located on the campus of City College of New York (CCNY) at 133rd Street and Convent Avenue in Upper Manhattan. It is being constructed in three phases: 1) Phases I and II will house a group of high-field magnetic resonance spectrometers (750, 800 and 900 at MHz); Phase I will be operational by March 31, 2002; and Phase II will be operational by December 31, 2002. This application is for Phase III funding only. It comprises 10,000 sq. ft. to house three cryo EM at 120 kV, 200 kV, and 300 kV, and necessary ancillary activities. Thesaurus Terms: There are no thesaurus terms on file for this project.Institution: NEW YORK STRUCTURAL BIOLOGY CENTER
- CONVENT AVE NEW YORK, NY 10027
Grant Number: 5P41GM066354-02
PI Name: COWBURN, DAVID A. PI Email: cowburn@nysbc.org PI Title: PRESIDENT & CEO Project Title: 900 MHz NMR Spectrometer for Structural Biology Abstract: DESCRIPTION: 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 funds for part 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. Thesaurus Terms: biomedical equipment purchase, biomedical resource, nuclear magnetic resonance spectroscopy, structural biology membrane protein, nucleic acid, protein Institution: NEW YORK STRUCTURAL BIOLOGY CENTER- CONVENT AVE NEW YORK, NY 10027
Grant Number: 2R01GM047021-13A2
PI Name: COWBURN, DAVID A. PI Email: cowburn@nysbc.org PI Title: PRESIDENT & CEO Project Title: Structural Biology of Protein Kinases Abstract: DESCRIPTION (provided by applicant): This proposal will extend the knowledge of the structure, in solution, of the protein kinases, Csk, and Abelson (Abl), and their complexes in intracellular signal transduction using contemporary NMR and molecular biology approaches, and new technologies. The last will extend segmental labeling using expressed protein ligation, and direct determination of segmental motion of multidomain proteins from relaxation studies and from residual dipolar couplings. The kinases to be studied and their close homologs are key targets for increased understanding of signal transduction in processes associated with human health - immune system signaling, the DNA damage response, osteoclast differentiation, and general cellular growth and differentiation control. These kinases are prototypical of many signaling molecules in that it consists of multiple functional modules, some of which are independently folded structural domains, and these interact both among themselves, and with other ligands, in complex ways which are not readily characterized by conventional structure determination methods. In this proposal, the focus will be on the medium resolution interaction of domains, understanding their role in modification reactions of phosphorylation, and dephosphorylation, the interaction of kinase control with ligands, substrates, adaptors, and the adjacent domains, and examination at high resolution in solution of those which are found amenable in solubility and complexity for complete structural and dynamic characterization. In understanding the role of individual domains and model systems, additional detailed studies will also be undertaken on dynamic properties of multiple domain systems, like Abl SH(32) and Csk(32) by both 15N relaxation methods, and residual dipolar coupling methods; dynamic studies of enzymatically inactivated analogs of down regulated Src; and surveys of the formation of the enzymatic activating complexes of Csk, Src, and their associated phosphatases. Institution: NEW YORK STRUCTURAL BIOLOGY CENTER- CONVENT AVE NEW YORK, NY 10027
Previous support Cowburn Patents
- DavidCowburn.doc: Brief background
- CRISP_-_Computer_Retrieval_of_Information_on_Scientific_Proje...pdf: CRISP retrieval
- Full Biographical Sketch
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