Kulczyk, A, Yang, J.-C. & Neuhaus, D. (2004)
Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIa. J.
Mol Biol. 341, 723-738.
Argentaro, A., Yang, J.-C., Chapman, L., Kowalczyk, M.S., Gibbons, R.J., Higgs, D.R., Neuhaus, D. & Rhodes, D.(2007)
Structural consequences of disease-causing mutations in the ATRXDNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX.
Proc. Natl. Acad. Sci U.S.A. 104, 11939-11944.
van Roon, A.M.M., Loening, N.M., Obayashi, E., Yang, J.-C., Newman, A.J.,Hernandez, H., Nagai K. & Neuhaus, D. (2008)
Solution structure of the U2snRNP protein RDS3p reveals a knotted zinc finger motif.
Proc. Natl. Acad. Sci. U.S.A. 105, 9621-9626.
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Group Members
- Ji-Chun Yang
- Sebastian Eustermann
- Wing-Fung (Wilfred) Wu
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Nuclear magnetic resonance (NMR) spectroscopy is the most powerful physical method available for the study of molecular structure in the solution state, probing interactions between nuclei to reveal their spatial relationships and dynamic properties.
By using multi-pulse, multi-dimensional NMR in conjunction with isotope labelling using 15N and 13C, detailed three-dimensional solution structures of macromolecules and complexes of 30KDa and higher are made accessible to study. More recently, partial deuteration and new experiments have extended this range still further.
The LMB has 300, 500, 600 and 800 MHz NMR spectrometers. We have been using these to determine structures of a variety of proteins, including a number of zinc finger domains and components from the ATP synthase enzyme.
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Protein function depends crucially on specific interactions with target molecules, and NMR is uniquely well-placed to help in understanding the underlying basis of such recognition in solution.
We are working on structures of a number of complexes, including particularly complexes of several DNA-binding proteins, and in collaboration with Murray Stewart, protein-protein interactions relevant to understanding the mechanism of nuclear import and export.
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Group Leaders 
