期刊
BIOPHYSICAL JOURNAL
卷 95, 期 6, 页码 2880-2894出版社
BIOPHYSICAL SOC
DOI: 10.1529/biophysj.107.120832
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资金
- ESRF
- Medical Research Council
- Howard Hughes Medical Institute
- Russian Foundation for Basic Research
- European Molecular Biology Laboratory
- Medical Research Council [G0100150] Funding Source: researchfish
- MRC [G0100150] Funding Source: UKRI
A direct modeling approach was used to quantitatively interpret the two-dimensional x-ray diffraction patterns obtained from contracting mammalian skeletal muscle. The dependence of the calculated layer line intensities on the number of myosin heads bound to the thin. laments, on the conformation of these heads and on their mode of attachment to actin, was studied systematically. Results of modeling are compared to experimental data collected from permeabilized fibers from rabbit skeletal muscle contracting at 5 degrees C and 30 degrees C and developing low and high isometric tension, respectively. The results of the modeling show that: i), the intensity of the first actin layer line is independent of the tilt of the light chain domains of myosin heads and can be used as a measure of the fraction of myosin heads stereospecifically attached to actin; ii), during isometric contraction at near physiological temperature, the fraction of these heads is similar to 40% and the light chain domains of the majority of them are more perpendicular to the. lament axis than in rigor; and iii), at low temperature, when isometric tension is low, a majority of the attached myosin heads are bound to actin nonstereospecifically whereas at high temperature and tension they are bound stereospecifically.
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