Open AccessX -ray studies of the molecular structure of myosin
Author(s) -
W. T. Astbury,
Sylvia Dickinson
Publication year - 1940
Publication title -
proceedings of the royal society of london. series b, biological sciences
Language(s) - English
Resource type - Journals
eISSN - 2053-9193
pISSN - 0080-4649
DOI - 10.1098/rspb.1940.0041
Subject(s) - myosin , keratin , folding (dsp implementation) , chemistry , polypeptide chain , biophysics , crystallography , biochemistry , biology , enzyme , genetics , structural engineering , engineering
The X-ray and elastic properties of myosin are found to resemble most closely, not those of natural keratin, but those of keratin that has suffered breakdown among the cross-linkages (including disulphide bridges) of the polypeptide grid. The supercontraction of myosin cannot be explained as due simply to disorientation of long thin units: it must involve a further folding of the polypeptide chain system. The fact that myosin and keratin are similar in both molecular configuration and elastic properties is discussed in the light of recent X-ray and chemical findings, and the X-ray interpretation is given of the denaturation of myosin.