| Literature DB >> 8031829 |
G F Elliott1, C R Worthington.
Abstract
A new molecular model is proposed for muscle contraction, that involves the electrical charging of the long (C-terminal) alpha-helical part of the head of the myosin molecule (S1) while the head is attached to actin; as it charges the alpha-helical part moves in the radial electric field between the filaments. The alpha-helical part snaps back when the myosin molecule is discharged electrically, at the moment that ATP binds to the active enzymatic site. This snap-back model explains several puzzling phenomena in contractility, as well as providing a physical explanation for the origin of an impulsive force that drives muscle contraction.Entities:
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Year: 1994 PMID: 8031829 DOI: 10.1016/0304-4165(94)90124-4
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002