[Thin filament elasticity and its role in the muscle contraction].
The available experimental methods do not allow one to establish unambiguously the molecular structural events during muscle contraction. To resolve the existing controversies, I have devised an unconventional original computer program. The new approach allows the reconstruction of the hexagonal lattice of the sarcomere for different muscle states and verification of the structure by comparison of the calculated Fourier spectra with the real diffraction patterns. Previously, by the use of this approach, the real structure of a myosin filament from vertebrate striated muscle has been reconstructed (http://zope.ibib.waw.pl/pspk). In this work, a reconstruction for the thin filament is presented for three states: relaxed, after activation, and during contraction. Good consistency of the calculated Fourier spectra with the real diffraction patterns available in the literature suggests that the thin filament, due to flexibility, plays an active part in muscle contraction, as myosin cross-bridges do.
Skubiszak
L
L
D008841:Actin Cytoskeleton / Q000737:chemistry*; D000199:Actins / Q000737:chemistry; D003198:Computer Simulation; D005583:Fourier Analysis; D009119:Muscle Contraction; D009126:Muscle Relaxation; D014335:Tropomyosin / Q000737:chemistry; D014336:Troponin / Q000737:chemistry; D014961:X-Ray Diffraction
D000199:Actins; D014335:Tropomyosin; D014336:Troponin