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Structural Biology

Martin Webb group project:

Myosins: the relationship between ATP hydrolysis and mechanical events

Biosensors and novel fluorescent nucleotides, developed in this laboratory, are being used as an approach to understand mechanochemical coupling in myosin-based motors. We are investigating how the biochemical ATP hydrolysis cycle is modified between actomyosin and more ordered systems of actin and myosin, to understand the role of particular steps in the cycle are involved in mechanical responses. We are also involved in a project to understand the mechanism of myosin V, using one of the fluorescent nucleotides with a diethylaminocoumarin attached to the ribose of ATP (shown below).

Myosin V

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Selected publications

West, TG; Hild, G; Siththanandan, VB; Webb, MR; Corrie, JET and Ferenczi, MA (2009)
Time course and strain dependence of ADP release during contraction of permeabilized skeletal muscle fibers.
Biophysical Journal 96, 3281-94 PubMed abstract
Sakamoto, T; Webb, MR; Forgacs, E; White, HD and Sellers, JR (2008)
Direct observation of the mechanochemical coupling in myosin Va during processive movement.
Nature 455, 128-32 PubMed abstract
Forgacs, E; Cartwright, S; Sakamoto, T; Sellers, JR; Corrie, JET; Webb, MR and White, HD (2008)
Kinetics of ADP dissociation from the trail and lead heads of actomyosinV following the power-stroke.
Journal of Biological Chemistry 283, 766-773 PubMed abstract
Lionne, C; Iorga, B; Candau, R; Piroddi, N; Webb, MR; Belus, A; Travers, F and Barman, T (2002)
Phosphate release is the rate limiting step on the ATPase of psoas myofibrils, prevented from shortening by chemical cross-linking.
Biochemistry 41, 13297-13308