Time-resolved and Stopped-Flow NMR

NMR is one of the few analytical techniques which is capable of giving truly atomic resolution. I am interested in developing NMR-based methods which enable kinetic information to be obtained, both for chemical and biochemical reactions.

An example of this has been the development of a stopped-flow mixing accessory for a standard NMR spectrometer. This device is capable of producing complete and homogeneous mixing within 50 ms following the injection event. This device has been used in a number of studies of protein folding. However, its utility is applicable to any binary mixing scheme.

I am also interested in developing time-resolved NMR methods which provide access to kinetic parameters. This includes the modification of "traditional" NMR experiments to suit the systems under investigation.

Key publications

  1. K. H. Mok, L. T. Kuhn, M. Goez, I. J. Day, J. C. Lin, N. H. Andersen, and P. J. Hore.
    A pre-exisiting hydrophobic collapse in the unfolded state of an ultrafast folding protein.
    Nature, 447(7140):106-109, 2007. [ DOI ]
  2. K. H. Mok, T. Nagashima, I. J. Day, J. A. Jones, C. J. V. Jones, C. M. Dobson, and P. J. Hore.
    Rapid sample-mixing technique for transient NMR and Photo-CIDNP spectroscopy: Applications to real-time protein folding.
    J. Am. Chem. Soc., 125(41):12484-12492, 2003. [ DOI ]
  3. S. M. Harper, L. C. Neil, I. J. Day, P. J. Hore, and K. H. Gardner.
    Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy.
    J. Am. Chem. Soc., 126(11):3390-3391, 2004. [ DOI ]