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Optimal 2H rf pulses and 2H-13C cross-polarization methods for solid-state 2H MAS NMR of perdeuterated proteins.
J. Phys. Chem. Lett. 2, 1289-1294 (2011)
We present a novel concept for if pulses and optimal control designed cross-polarization experiments for quadrupolar nuclei. The methods are demonstrated for (2)H CP-MAS and (2)H multiple-pulse NMR of perdeuterated proteins, for which sensitivity enhancements up to an order of magnitude are presented relative to commonly used approaches. The so-called RESPIRATION rf pulses combines the concept of short broad-band pulses with generation of pulses with large flip angles through distribution of the rf pulse over several rotor echoes. This lead to close-to-ideal rf pulses, facilitating implementation of experiments relying on the ability to realize high-performance 90 and 180 degrees pulses, as, for example, in refocused INEPT and double-to-single quantum coherence experiments, or just pulses that provide a true representation of the quadrupolar powder pattern to extract information about the structure or dynamics. The optimal control (2)H ->(13)C CP-MAS method demonstrates transfer efficiencies up to around 85% while being extremely robust toward rf inhomogeneity and resonance offsets.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
1 systems; quadrupole-echo; correlation spectroscopy; distance measurements; deuterated proteins; amyloid fibrils; resolution; dynamics; spectra; design
e-ISSN
1948-7185
Quellenangaben
Volume: 2,
Issue: 11,
Pages: 1289-1294
Publisher
American Chemical Society (ACS)
Publishing Place
Washington, USA
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)