Molecular Contractility Research

Our interests range from the structure and function of the contractile apparatus of muscle; the myofibril, to the structure and functions of the plethora of myosins discovered over the last 10 years, in non-muscle cells. We use a wide range of techniques such as: wet biochemistry (protein isolation, expression and characterisation), biophysical methods (eg analytical ultracentrifugation, AFM), light microscopy (confocal, time-lapse fluorescence and deconvolution) electron microscopy, including time-resolved cryo-EM, molecular genetic tools and cell biology (tissue culture, live cell imaging) to investigate the structure and function of the muscle proteins myosin, titin and actin. Our research forms part of the major effort in structural biology at Leeds.

This is an animation of an atomic model of the head of the myosin 2 molecule docked onto actin in two conformations thought to mimic the start (shown) and end of the power stroke. (Shockwave plugin available here).

Or you can download the movie (6.0MB)

Using electron microscopy and single particle image processing we have elucidated the structure of myosin 5 attached to actin and the structure and power stroke of dynein - both recently published in Nature.

click here for myosin v results

Motion of myosin V molecules on actin.

We also investigate cell behaviour using time-lapse phase microscopy, DRIMAPS (with Dr Graham Dunn at King's College London), and we use time-lapse fluorescence microscopy and Total Internal Reflection Fluorescence Microscopy (TIRFM) to image single molecules of GFP-myosin (with Dr Justin Molloy at Nat Inst for Med Res).

crawling myoblasts imaged using Digitally Recorded Interference Microscopy with Automatic Phase Shifting (DRIMAPS)

Crawling myoblasts imaged using
Digitally Recorded Interference Microscopy
with Automatic Phase Shifting (DRIMAPS)

(with Graham Dunn, KCL)

(Professor John Trinick, Dr Peter Knight, Dr Michelle Peckham and Dr Stan Burgess)

111Mb, Quicktime 6Mb, Quicktime


We are actively recruiting post-docs and graduate students to join our group to contribute to a range of projects on myosin, actin and titin. The Leeds Muscle Group is lively and friendly and interested in application of state-of-the-art methods to important questions in muscle and motility.  A background in biological sciences is not essential and we are also keen to recruit from other disciplines such as physics or mathematics.


The Dynein homepage is now at



111Mb, Quicktime 6Mb, Quicktime