Optimal control based NCO and NCA experiments for spectral assignment in biological solid-state NMR spectroscopy.


Journal Article

We present novel pulse sequences for magic-angle-spinning solid-state NMR structural studies of (13)C,(15)N-isotope labeled proteins. The pulse sequences have been designed numerically using optimal control procedures and demonstrate superior performance relative to previous methods with respect to sensitivity, robustness to instrumental errors, and band-selective excitation profiles for typical biological solid-state NMR applications. Our study addresses specifically (15)N to (13)C coherence transfers being important elements in spectral assignment protocols for solid-state NMR structural characterization of uniformly (13)C,(15)N-labeled proteins. The pulse sequences are analyzed in detail and their robustness towards spin system and external experimental parameters are illustrated numerically for typical (15)N-(13)C spin systems under high-field solid-state NMR conditions. Experimentally the methods are demonstrated by 1D (15)N-->(13)C coherence transfer experiments, as well as 2D and 3D (15)N,(13)C and (15)N,(13)C,(13)C chemical shift correlation experiments on uniformly (13)C,(15)N-labeled ubiquitin.

Full Text

Cited Authors

  • Kehlet, C; Bjerring, M; Sivertsen, AC; Kristensen, T; Enghild, JJ; Glaser, SJ; Khaneja, N; Nielsen, NC

Published Date

  • October 2007

Published In

Volume / Issue

  • 188 / 2

Start / End Page

  • 216 - 230

PubMed ID

  • 17681479

Pubmed Central ID

  • 17681479

Electronic International Standard Serial Number (EISSN)

  • 1096-0856

International Standard Serial Number (ISSN)

  • 1090-7807

Digital Object Identifier (DOI)

  • 10.1016/j.jmr.2007.06.011


  • eng