Abstract
By averaging the α-helix parameters of Chou & Fasman (1974) over extended segments of the α-tropomyosin sequence, the maxima and minima of the 7-fold periodicity initially detected by Parry (1975) are observed to correspond approximately to the outer non-polar positive zones of the alternating β and α actin binding sites, respectively, described by McLachlan & Stewart (1976 a). The periodicity is well developed in the NH 2-terminal and central regions of the molecule but becomes progressively less distinctive towards the COOH-terminus. Initial cleavage points by trypsin and chymotrypsin occur close to minima in the averaged α-helical parameters.
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