This proposal requests continued support for the MIT/Harvard Center for Magnetic Resonance (CMR) located at the Francis Bitter Magnet Laboratory, MIT, a joint effort between MIT and Harvard Medical School. During the coming five-year period we plan significant upgrades of existing equipment, acquisition of new instrumentation, and research initiatives in several new areas. Specifically, the P41 grant will continue to support an exciting core research program in magnetic resonance based structural biology focused on studies of membrane proteins, translation initiation, amyloid, new high frequency microwave technology for magnetic, methods for non-uniform sampling and dynamic nuclear polarization, and high temperature superconducting magnets for NMR. In addition, we will be developing new instrumentation as follows: (1) T-locks for the solution 750 and 900 MHz spectrometers; (2) upgrading of a 460 GHz/700 MHz dynamic nuclear polarization (DNP)/NMR spectrometer; (3) design and construction of helium recirculation system for low temperature DNP experiments in the 10-60 K regime; (4) design and construction of a new generation of MAS probes that are balanced on all channels; (5) design and construction of the next generation of NMR console on a chip. The research of the five TR&D's will implement new technology for NUS, for preparation and analysis of membrane protein structures, studies of sedimented samples, high frequency MAS for membrane and amyloid protein, improving resolution at low temperatures and 17-O labeling and spectroscopy.

Public Health Relevance

The CMR consists of a cluster of high field NMR and EPR spectrometers devoted to long term experiments in structural biology. In addition, many new exciting applications are being pursued particularly in the area of membrane protein and amyloid fibril structure. The CMR is heavily involved in collaborations and is open to the user community interested in high field magnetic resonance.

Agency
National Institute of Health (NIH)
Institute
National Institute of Biomedical Imaging and Bioengineering (NIBIB)
Type
Biotechnology Resource Grants (P41)
Project #
5P41EB002026-40
Application #
8856233
Study Section
Special Emphasis Panel (ZEB1-OSR-E (J2))
Program Officer
Sastre, Antonio
Project Start
1976-05-30
Project End
2019-04-30
Budget Start
2015-05-01
Budget End
2016-04-30
Support Year
40
Fiscal Year
2015
Total Cost
$1,116,652
Indirect Cost
$344,272
Name
Massachusetts Institute of Technology
Department
Type
Organized Research Units
DUNS #
001425594
City
Cambridge
State
MA
Country
United States
Zip Code
02139
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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