Asynchronous through-bond homonuclear isotropic mixing: application to carbon–carbon transfer in perdeuterated proteins under MAS-Reference-Cited by-同舟云学术

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Asynchronous through-bond homonuclear isotropic mixing: application to carbon–carbon transfer in perdeuterated proteins under MAS

Published:2015-08-30 Issue:3 Volume:63 Page:245-253
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Kulminskaya Natalia,Vasa Suresh Kumar,Giller Karin,Becker Stefan,Linser Rasmus

Funder

Deutsche Forschungsgemeinschaft

Verband der Chemischen Industrie

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s10858-015-9980-1.pdf

Reference56 articles.

1. Agarwal V, Reif B (2008) Residual methyl protonation in perdeuterated proteins for multi-dimensional correlation experiments in MAS solid-state NMR spectroscopy. J Magn Reson 194:16–24

2. Agarwal V, Diehl A, Skrynnikov N, Reif B (2006) High resolution 1H detected 1H,13C correlation spectra in MAS solid-state NMR using deuterated proteins with selective 1H,2H isotopic labeling of methyl groups. J Am Chem Soc 128:12620–12621

3. Agarwal V et al (2014) De novo 3D structure determination from sub-milligram protein samples by solid-state 100 kHz MAS NMR spectroscopy. Angew Chem Int Ed 53:12253–12256

4. Akbey U, Oschkinat H, van Rossum BJ (2009) Double-nucleus enhanced recoupling for efficient 13C MAS NMR correlation spectroscopy of perdeuterated proteins. J Am Chem Soc 131:17054

5. Asami S, Schmieder P, Reif B (2010) High resolution 1H-detected solid-state NMR spectroscopy of protein aliphatic resonances: access to tertiary structure information. J Am Chem Soc 132:15133–15135

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