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==Introduction==
==Introduction==
[[Image:Actin myosin anim.gif]]
[[Image:Actin myosin anim.gif]]
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Muscle contraction is achieved by the sliding of myosin filament (thick filament) and actin filament (thin filament). As the major constituent of myosin filament, a myosin molecule is a multifunctional protein, which has a ATP catalytic site and a actin binding site on each of the globular subfragment-1 unit. With the presence of Ca and Mg, ATP ís able to be hydrolyzed and triggers following myosin-actin detachment, reattachment and power stroke. This process transformed chemical energy to mechanical force.
==Different Structural Conformations of the Scallop Myosin Head==
==Different Structural Conformations of the Scallop Myosin Head==

Revision as of 07:27, 15 May 2014

This Sandbox is Reserved from 01/04/2014, through 30/06/2014 for use in the course "510042. Protein structure, function and folding" taught by Prof Adrian Goldman, Tommi Kajander, Taru Meri, Konstantin Kogan and Juho Kellosalo at the University of Helsinki. This reservation includes Sandbox Reserved 923 through Sandbox Reserved 947.
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Contents

Scallop myosin head in its rigor state, detached state and pre power stroke state

Introduction

Image:Actin myosin anim.gif Muscle contraction is achieved by the sliding of myosin filament (thick filament) and actin filament (thin filament). As the major constituent of myosin filament, a myosin molecule is a multifunctional protein, which has a ATP catalytic site and a actin binding site on each of the globular subfragment-1 unit. With the presence of Ca and Mg, ATP ís able to be hydrolyzed and triggers following myosin-actin detachment, reattachment and power stroke. This process transformed chemical energy to mechanical force.

Different Structural Conformations of the Scallop Myosin Head

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References

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