期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：9
页码：5559-5563
DOI：10.1073/pnas.78.9.5559
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The effect of strain on the equatorial x-ray diffraction pattern of glycerinated rabbit psoas fibers was studied in the rigor (ATP free) state. Strains between 30 and 100 A per half sarcomere, measured directly by laser diffraction, did not change the intensity ratio, (10)/ . (11). Because the intensity ratio depends on the distribution of mass within the myofilament lattice, the negative result indicates that strain does not change the angle of attachment of the subfragment 1 (S1) moiety of the myosin molecule to the actin filament. The effect of strain on the ordering of the actin filaments also was considered and judged to be negligible.
