Protein solid-state NMR resonance assignments from (13C,13C) correlation spectroscopy

Karsten Seidel; Adam Lange; Stefan Becker; Colan E. Hughes; Henrike Heise; Marc Baldus

doi:10.1039/B411689E

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Proteinsolid-state NMR resonance assignments from (¹³C,¹³C) correlation spectroscopy

Karsten Seidel,^a Adam Lange,^a Stefan Becker,^a Colan E. Hughes,^a Henrike Heise^a and Marc Baldus*^a

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* Corresponding authors

^a Max-Planck-Institute for Biophysical Chemistry, Department for NMR-Based Structural Biology, Göttingen, Germany
E-mail: maba@mpibpc.mpg.de
Fax: +49 5512012202
Tel: +49 5512012212

Abstract

It is demonstrated that sequential resonance assignments can be obtained from (¹³C,¹³C) correlation spectroscopy on a uniformly labeled protein under magic angle spinning. The experiment relies on weak (C′,Cα) coupling conditions using a defined range of MAS rates and can be employed at arbitrary magnetic field strength.

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Article information

DOI: https://doi.org/10.1039/B411689E
Article type: Communication
Submitted: 30 Jul 2004
Accepted: 28 Sep 2004
First published: 08 Oct 2004

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Phys. Chem. Chem. Phys., 2004,6, 5090-5093

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Protein solid-state NMR resonance assignments from (¹³C,¹³C) correlation spectroscopy

K. Seidel, A. Lange, S. Becker, C. E. Hughes, H. Heise and M. Baldus, Phys. Chem. Chem. Phys., 2004, 6, 5090 DOI: 10.1039/B411689E

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