Dr. S. Djordjevic is acknowledged for providing TEV-protease. Expression constructs of T4 lysozyme mutants were kindly provided by Prof. L. E. Kay and Prof. F. W. Dahlquist. We acknowledge the Medical Research Council and the National Institute for Medical Research for access to the 800 MHz spectrometer. N.D.W. acknowledges FEBS for a long-term postdoctoral fellowship. This research is supported by the Biotechnology and Biological Sciences Research Council (BBSRC). D.F.H. is a BBSRC David Phillips Fellow.
Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH†
Article first published online: 10 FEB 2013
© 2013 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Angewandte Chemie International Edition
Volume 52, Issue 11, pages 3145–3147, March 11, 2013
How to Cite
Werbeck, N. D., Kirkpatrick, J. and Hansen, D. F. (2013), Probing Arginine Side-Chains and Their Dynamics with Carbon-Detected NMR Spectroscopy: Application to the 42 kDa Human Histone Deacetylase 8 at High pH. Angew. Chem. Int. Ed., 52: 3145–3147. doi: 10.1002/anie.201209385
- Issue published online: 7 MAR 2013
- Article first published online: 10 FEB 2013
- Manuscript Revised: 8 JAN 2013
- Manuscript Received: 23 NOV 2012
- Funded Access
- Biotechnology and Biological Sciences Research Council (BBSRC)
- histone deacetylases;
- NMR spectroscopy;
- protein dynamics;
- spin relaxation
Arginine side-chains play a distinct role because of their high pKa and perpetual positive charge. An NMR method is presented, based on carbon-detected 13Cζ–15Nε correlation spectra, which allows probing the arginine side-chains and their dynamics at neutral-to-high pH. The methodology is demonstrated on human histone deacetylase 8.