Study of tropomyosin labelled with a fluorescent probe by pulse fluorimetry in polarized light. Interaction of that protein with troponin and actin.

Tropomyosin has been labelled with a fluorescent probe N-iodoacetyl-N'-(5-sulfo-1-naphthyl)-ethylenediamine which is presumed to bind preferentially to the unique reactive cysteine residue of the alpha chain. Anisotropy decay measurements show that tropomyosin monomer and polymer are flexible molecules. This flexibility decreases when troponin interacts with tropomyosin, and is partially restored by a micromolar concentration of Ca2+.