Abstract
Definition of the molecular mechanisms in muscle contraction and its regulation entails a description of how the components of the organised assembly of proteins first dock with their substrates/partners, then interact and transmit information through the molecular array. Crosslinking studies and experiments with proteolysed fragments of the myosin head (subfragment 1, S1) from a variety of laboratories [e.g. Chaussepied et al., 1986a; Sutoh, 1983] have indicated the approximate regions of the molecule involved in complex formation. In order to define precisely the exact locations of these interfaces we have synthesized peptides based on the S1 sequence and tested these for their ability to bind to actin and influence its biological properties. Such chemical synthesis allows small regions of the parent protein, usually not obtainable by proteolytic or chemical digestion, to be examined in isolation.
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Trayer, I.P., Keane, A.M., Murad, Z., Rüegg, J.C., Smith, K.J. (1991). The Use of Peptide Mimetics to Define the Actin-Binding Sites on the Head of the Myosin Molecule. In: Rüegg, J.C. (eds) Peptides as Probes in Muscle Research. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76409-7_7
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DOI: https://doi.org/10.1007/978-3-642-76409-7_7
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