Abstract
Summary Conditions are described for the nearly quantitative removal of residues 274–284 from the COOH-terminus of rabbit cardiac tropomyosin. The product is monomeric (Mr = 64,000) even at low ionic strength. The circular dichroism melting profile is only marginally different from the intact protein. The failure of the non-polymerizable tropomyosin to bind to F-actin, even at elevated MgCl2 concentrations, illustrates the importance of the head-to-tail interaction of tropomyosin molecules in their cooperative binding to the thin filament structure.
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