Abstract

This proposal requests continued support for the MIT/Harvard Center for Magnetic Resonance (CMR) located at the Francis Bitter Magnet Laboratory, MIT (EB002026). During the coming five-year period we plan significant upgrades of existing equipment, acquisition of new instrumentation, and research initiatives in several new areas. During the proposed five year grant period, we plan to initiate or complete construction or acquisition of the following new pieces of equipment, which will be integrated into the facility. These instruments will include the following: (1) a 460 GHz/700 MHz dynamic nuclear polarization (DNP)/NMR spectrometer;(2) an 800 MHz/89 mm NMR primarily for solids and conversion of the 750/62 to a solution spectrometer;(3) a 140 GHz gyroamplifier for time domain DNP and EPR experiments;(4) a 600 MHz/125 mm spectrometer for temperature jump DNP experiments. This will entail construction of a 395 GHz gyrotron oscillator for the DNP experiments;(5) a helium recirculation system for MAS experiments in the 20-30 K regime;(6) a tunable 330 GHz gyrotron oscillator that will be interfaced to an existing 500/104 spectrometer;(7) a commercial 9 GHz time domain EPR for distance measurements. In addition we will continue the strong core, collaborative and user research programs. Scientific topics include membrane proteins, signaling, metabolomics, and amyloid proteins associated with disease.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Biomedical Imaging and Bioengineering (NIBIB)
Type
Biotechnology Resource Grants (P41)
Project #
5P41EB002026-37
Application #
8272574
Study Section
Special Emphasis Panel (ZRG1-BCMB-N (40))
Program Officer
Sastre, Antonio
Project Start
1976-05-01
Project End
2014-04-30
Budget Start
2012-05-01
Budget End
2013-04-30
Support Year
37
Fiscal Year
2012
Total Cost
$1,114,097
Indirect Cost
$416,910

  Institution

Name
Massachusetts Institute of Technology
Department
Type
Organized Research Units
DUNS #
001425594
City
Cambridge
State
MA
Country
United States
Zip Code
02139

  Publications

Chhabra, Sandeep; Fischer, Patrick; Takeuchi, Koh et al. (2018) 15N detection harnesses the slow relaxation property of nitrogen: Delivering enhanced resolution for intrinsically disordered proteins. Proc Natl Acad Sci U S A 115:E1710-E1719
Mallis, Robert J; Arthanari, Haribabu; Lang, Matthew J et al. (2018) NMR-directed design of pre-TCR? and pMHC molecules implies a distinct geometry for pre-TCR relative to ??TCR recognition of pMHC. J Biol Chem 293:754-766
Hagn, Franz; Nasr, Mahmoud L; Wagner, Gerhard (2018) Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR. Nat Protoc 13:79-98
Fu, Qingshan; Shaik, Md Munan; Cai, Yongfei et al. (2018) Structure of the membrane proximal external region of HIV-1 envelope glycoprotein. Proc Natl Acad Sci U S A 115:E8892-E8899
Hjortness, Michael K; Riccardi, Laura; Hongdusit, Akarawin et al. (2018) Abietane-Type Diterpenoids Inhibit Protein Tyrosine Phosphatases by Stabilizing an Inactive Enzyme Conformation. Biochemistry 57:5886-5896
Coote, Paul W; Robson, Scott A; Dubey, Abhinav et al. (2018) Optimal control theory enables homonuclear decoupling without Bloch-Siegert shifts in NMR spectroscopy. Nat Commun 9:3014
Wittmann, J J; Can, T V; Eckardt, M et al. (2018) High-precision measurement of the electron spin g factor of trapped atomic nitrogen in the endohedral fullerene N@C60. J Magn Reson 290:12-17
Ji, X; Can, T V; Mentink-Vigier, F et al. (2018) Overhauser effects in non-conducting solids at 1.2?K. J Magn Reson 286:138-142
Iadanza, Matthew G; Silvers, Robert; Boardman, Joshua et al. (2018) The structure of a ?2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism. Nat Commun 9:4517
Liao, Shu Y; Lee, Myungwoon; Hong, Mei (2018) Interplay between membrane curvature and protein conformational equilibrium investigated by solid-state NMR. J Struct Biol :

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