NMR spectroscopy bridges physics and biology. We are developing new methods to extend the applicability of NMR to larger biological systems.
- new sparse sampling methods
- new methods for measuring paramagnetic effects in proteins
- development of protein structure determination strategies
- Yagi, H., Pilla, K. B., Maleckis, A., Graham, B., Huber, T. and Otting, G. (2013) 3D protein fold determination from pseudocontact shifts of backbone amides. Structure 21, 883-890.
- Shishmarev, D., Wang, Y., Mason, C. E., Su, X.-C., Oakley, A. J., Graham, B., Huber, T., Dixon, N. E. and Otting, G. (2013) Intramolecular binding mode of the C-terminus of E. coli single-stranded DNA binding protein (SSB) determined by nuclear magnetic resonance spectroscopy. Nucleic Acids Res. 42, 2750-2757.