An unexpectedly large working stroke from chymotryptic fragments of myosin II |
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Authors: | Molloy J E Kendrick-Jones J Veigel C Tregear R T |
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Affiliation: | Department of Biology, University of York, UK. |
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Abstract: | Recent structural evidence indicates that the light chain domain of the myosin head (LCD) bends on the motor domain (MD) to move actin. Structural models usually assume that the actin-MD interface remains static and the possibility that part of the myosin working stroke might be produced by rotation about the acto-myosin interface has been neglected. We have used an optical trap to measure the movement produced by proteolytically shortened single rabbit skeletal muscle myosin heads (S-1(A1) and S-1(A2)). The working stroke produced by these shortened heads was more than that which the MD-LCD bend mechanism predicts from the full-length (papain) S-1’s working stroke obtained under similar conditions. This result indicates that part of the working stroke may be caused by motor action at the actin-MD interface. |
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Keywords: | Myosin Working stroke Optical trap Motor Muscle Single molecule |
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