Myosin subfragment-1 attachment to actin. Expected effect on equatorial reflections.
The characteristic equatorial X-ray pattern from a relaxed vertebrate skeletal muscle changes when the muscle is activated. In particular, there is a simultaneous decrease in the intensity of the first reflection (I10) and increase in the intensity of the second (I11). This observed change is almost reciprocal. When compared with the predictions of computer modeling, it produces a strong argument that the intensity change is due to a redistribution of myosin heads (myosin subfragment-1 or S-1), which results from the formation and configuration changes of actin-myosin links. Computer modeling shows that different actin-S-1 configurations will give different numerical values for I10 and I11, assuming the same number of attachments. For a given configuration, the intensity changes are a nonlinear function of attachment number, so that direct scaling of force to reflection intensity may be difficult. Data from active muscle are consistent with the notion that in different states of active muscle, i.e. shortening or isometric, there are different average configurations of actin-myosin attachment and different numbers of actin-myosin links.
D000199:Actins / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D014961:X-Ray Diffraction
D000199:Actins; D010446:Peptide Fragments; D009218:Myosins