Abstract
PARAMYOSIN, a fibrous protein which has so far only been found in the muscles of invertebrates, gives an X-ray pattern with sharp 1.5 and 5.1 Å meridional and diffuse 10 Å near-equatorial reflexions and so is classified with α-keratin, myosin and fibrinogen as an α-fibrous protein. The X-ray patterns of these proteins differ, however, in the low-angle region where the pattern may be indexed on a repeat of 198 Å for α-keratin1, 420 Å for striated muscle2, 226 Å for fibrinogen3 and 725 Å for paramyosin4. The only one of these low-angle patterns which is clearly understood is that of paramyosin which may be interpreted in terms of either the two-dimensional net shown in Fig. 1(a) or a helix5. Electron micrographs have shown a two-dimensional pattern of spots6 similar to the lattice in Fig. 1(a) where the axial repeat is 725 Å, and this is reduced to 145 Å in axial projection (Fig. 1(b)). This communication reports a pseudo-repeat of 29 Å in axial projection which shows up when the paramyosin is treated with silver.
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MILLER, A. Short Pseudo-repeat in Paramyosin. Nature 207, 524–525 (1965). https://doi.org/10.1038/207524a0
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DOI: https://doi.org/10.1038/207524a0
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