... understanding life in molecular detail

Prof Peter Knight

Protein motors; Electron microscopy; Cell motility; Protein dynamics

What are the mechanisms used by proteins that function as motors to move cargoes inside cells or to produce external movements such as muscle contraction and the beating of flagella? What are the principles by which activity is regulated in these systems? How is the complex macromolecular complex of the muscle myofibril assembled and how does turnover of protein molecules occur within it?

Current major projects include:
  • Mechanisms of regulation of myosin activity
  • Properties and roles of single stable alpha helical domains
  • Molecular mechanism of dynein

I became fascinated by the molecular basis of muscle contraction as a result of being taught about it by Jean Hanson’s research group at King’s College London when I was an undergraduate. I joined that group for my PhD project and have stayed in the motor protein field ever since, studying several myosins and dyneins, actin and titin. I have used a range of experimental techniques to tease out the structural basis of motor protein activity, most recently concentrating on electron microscopy combined with single particle image processing. The particular advantage of this method for motor proteins is its ability to visualise the diversity of conformations that is key to the conversion of chemical energy into mechanical work.


Detailed research programme                  Close ▲

Selected Publications

  1. Imai, H., Shima, T., Sutoh, K., Walker, M. L., Knight, P. J., Kon, T. & Burgess, S. A. (2015). “Direct observation shows superposition and large scale flexibility within cytoplasmic dynein motors moving along microtubules.” Nature Commun. 6, 8179.

  2. Billington, N., Revill, D. J., Burgess, S. A., Chantler, P. D. and Knight, P. J. (2014). “Flexibility within the heads of muscle myosin-2 molecules.” J. Mol. Biol. 426, 894-907.

  3. Guzik-Lendrum, S., Heissler, S. M., Billington, N., Takagi, Y., Yang, Y., Knight, P. J., Homsher, E. and Sellers, J.R. (2013). “Mammalian myosin-18A, a highly divergent myosin.” J. Biol. Chem. 288, 9532-9548.

  4. Roberts, A. J., Malkova, B., Walker, M.L., Sakakibara, H., Numata, N., Kon, T., Ohkura, R., Edwards, T. A., Knight, P. J., Sutoh, K., Oiwa, K. and Burgess, S.A. (2012). “ATP-driven remodeling of the linker domain in the dynein motor.” Structure, 20, 1670-1680.