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Wei, D.* ; Akbey, Ü.* ; Paaske, B.* ; Oschkinat, H.* ; Reif, B. ; Bjerring, M.* ; Nielsen, N.C.*

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)
DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter 1 systems; quadrupole-echo; correlation spectroscopy; distance measurements; deuterated proteins; amyloid fibrils; resolution; dynamics; spectra; design
e-ISSN 1948-7185
Zeitschrift Journal of Physical Chemistry Letters, The
Quellenangaben Band: 2, Heft: 11, Seiten: 1289-1294 Artikelnummer: , Supplement: ,
Verlag American Chemical Society (ACS)
Verlagsort Washington, USA
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)