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Role of flexibility in heads of the myosin motor protein family

Reference	B13501
Principal Investigator / Supervisor	Professor Peter Knight
Co-Investigators / Co-Supervisors	Professor John Trinick
Institution	University of Leeds
Department	Institute of Membrane & Systems Biology
Funding type	Research
Value (£)	284,396
Status	Completed
Type	Research Grant
Start date	04/06/2001
End date	03/10/2004
Duration	40 months

Abstract

The myosin superfamily has approximatley 15 members, almost all having two heads that can each bind actin and split ATP. How the heads in a molecule work together to move along actin tracks is largely unknown, but in some cases a 'processive' walking mechanism is likely. Simultaneous binding of both heads to the same actin filament must induce large distortions, either in the heads or in the alpha-helical myosin tail where they are joined. We will use electron microscopy to study these distortions and flexibility in three myosins with widely differing roles and head lengths: myosin II (16 nm), myosin V (31 nm) and myosin X (intermediate). Frozen-hydrated and negatively stained specimens will be analysed by single particle image processing.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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