Abstract

Joint NIH-NSF support is requested for the purchase of a 600 MHz wide bore NMR spectrometer. The proposed instrumentation will support on going research involving membranes and membrane proteins (Smith and McLaughlin), protein folding (Raleigh) and structural analysis of catalysts, biopolymers and other chemical systems (Grey). Several factors at Stony Brook assure the productive use of the requested instrumentation. . The research groups of Smith, Raleigh and Grey have extensive experience in solid-state NMR with expertise in biological NMR and methods development. . The requested instrumentation is a key component of an NMR facility that is being created through a structural biology initiative at Stony Brook. The NMR facility and the structural biology program have strong university support. . There is a strong research emphasis on membranes, membrane proteins and signal transduction at Stony Brook. Roughly 25 research groups participate in a weekly seminar and discussion series. . Facility management and technical support will be assured through the expertise of Dr. Martine Ziliox, currently the sold-state NMR applications manager at Bruker Instruments in the United States. She will relocate to Stony Brook and run the NMR facility.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10RR013889-01
Application #
2803043
Study Section
Special Emphasis Panel (ZRG1-PB (01))
Program Officer
Tingle, Marjorie
Project Start
1999-04-15
Project End
2001-04-14
Budget Start
1999-04-15
Budget End
2001-04-14
Support Year
1
Fiscal Year
1999
Total Cost
Indirect Cost

  Institution

Name
State University New York Stony Brook
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
804878247
City
Stony Brook
State
NY
Country
United States
Zip Code
11794

  Publications

Leroy, Emilie; Defour, Jean-Philippe; Sato, Takeshi et al. (2016) His499 Regulates Dimerization and Prevents Oncogenic Activation by Asparagine Mutations of the Human Thrombopoietin Receptor. J Biol Chem 291:2974-87
Kimata, Naoki; Pope, Andreyah; Rashid, Dawood et al. (2015) Sequential structural changes in rhodopsin occurring upon photoactivation. Methods Mol Biol 1271:159-71
Eilers, Markus; Goncalves, Joseph A; Ahuja, Shivani et al. (2012) Structural transitions of transmembrane helix 6 in the formation of metarhodopsin I. J Phys Chem B 116:10477-89
Itaya, Miki; Brett, Ian C; Smith, Steven O (2012) Synthesis, purification, and characterization of single helix membrane peptides and proteins for NMR spectroscopy. Methods Mol Biol 831:333-57
Arakawa, Makoto; Chakraborty, Raja; Upadhyaya, Jasbir et al. (2011) Structural and functional roles of small group-conserved amino acids present on helix-H7 in the ?(2)-adrenergic receptor. Biochim Biophys Acta 1808:1170-8
Goncalves, Joseph A; South, Kieron; Ahuja, Shivani et al. (2010) Highly conserved tyrosine stabilizes the active state of rhodopsin. Proc Natl Acad Sci U S A 107:19861-6
Ahmed, Mahiuddin; Davis, Judianne; Aucoin, Darryl et al. (2010) Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils. Nat Struct Mol Biol 17:561-7
Hornak, Viktor; Ahuja, Shivani; Eilers, Markus et al. (2010) Light activation of rhodopsin: insights from molecular dynamics simulations guided by solid-state NMR distance restraints. J Mol Biol 396:510-27
Ahuja, Shivani; Hornak, Viktor; Yan, Elsa C Y et al. (2009) Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation. Nat Struct Mol Biol 16:168-75
Ahuja, Shivani; Eilers, Markus; Hirshfeld, Amiram et al. (2009) 6-s-cis Conformation and polar binding pocket of the retinal chromophore in the photoactivated state of rhodopsin. J Am Chem Soc 131:15160-9

Showing the most recent 10 out of 23 publications