Dynamic nuclear polarization in biomolecular solid state NMR : methods and applications in peptides and membrane proteins

Solid state NMR can probe structure and dynamics on length scales from the atomic to the supramolecular. However, low sensitivity limits its application in macromolecules. NMR sensitivity can be improved by dynamic nuclear polarization (DNP), in which electron polarization is transferred to nuclei. We present applications of magic angle spinning NMR that demonstrate its utility for the determination of structure at atomic resolution. We then present new techniques and instrumentation for DNP that permit these methods to be applied to larger systems such as membrane proteins. These applications rest on several advances in instrumentation: millimeter-wave sources and conduits of power to the sample; low-temperature MAS probes incorporating millimeter-wave transmission; cryogenics and pneumatic control systems. We describe a 380 MHz DNP spectrometer incorporating a 250 GHz gyrotron oscillator and present the theory and operation of a 460 GHz gyrotron at the second harmonic of electron cyclotron resonance. We have applied DNP to study trapped photo cycle intermediates of the archael membrane protein bacteriorhodopsin, a light-driven transmembrane ion pump.

Department dc:contributor.department

Massachusetts Institute of Technology. Dept. of Chemistry.

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2007

Author dc:creator

• Bajaj, Vikram Singh

Advisor dc:contributor.advisor

• Robert G. Griffin.

• Chemistry.

Statement dc:rights

• M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/1721.1/40874

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/40874