Muscle proteins - their actions and interactions

Holmes, Kenneth C.

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Muscle proteins - their actions and interactions

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Holmes, Kenneth C.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Holmes, K. C. (1996). Muscle proteins - their actions and interactions. Current Opinion in Structural Biology, 6(6), 781-789. Retrieved from http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd%3DRetrieve%26db%3DPubMed%26list_uids%3D8994878%26dopt%3DAbstract.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-3CAA-C

Abstract

Muscle contracts by the myosin cross-bridges rowing the actin filaments past the myosin filaments. In the past year many structural details of this mechanism have become clear. Structural studies indicate distinct states for myosin S1 in the rigor, ATP or down conformation and in the products complex (ADP.Pi) or up to state. Crystallographic studies substantiate this classification and yield details of the transformation. The isomerization up to down is the power stroke of muscle. This consists in the main of large changes of angle of the lever arm (at the distal part of the myosin head) which can account for an 11 nm power stroke