Binding of tropomyosin-troponin to actin increases filament bending stiffness.
Rheologic measurements show that the association of tropomyosin-troponin with actin filaments is responsible for the reduction of the internal chain dynamic and increase in the mechanical rigidity of actin filaments. Basing calculations on the linear relation between the plateau modulus, G(N)('), and bending modulus, kappa, I find that tropomyosin-troponin at r(AT) = 7 increases actin filament stiffness by approximately 50%. This is confirmed by dynamic light scattering. Further increases are observed at rising F-actin and constant tropomyosin-troponin concentrations. Tropomyosin-troponin also delays actin assembly and subsequent network formation and increases filament stiffness over time.
Goldmann
W H
WH
Departments of Pathology and Surgery, Children's Hospital, Boston, Massachusetts, 02115, USA.
D008841:Actin Cytoskeleton / Q000737:chemistry* / Q000378:metabolism; D000199:Actins / Q000378:metabolism*; D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D004548:Elasticity; D007700:Kinetics; D008027:Light; D008954:Models, Biological; D018583:Pliability; D011485:Protein Binding; D011487:Protein Conformation; D012212:Rheology; D012542:Scattering, Radiation; D014335:Tropomyosin / Q000378:metabolism*; D014336:Troponin / Q000378:metabolism*; D014783:Viscosity
D000199:Actins; D001704:Biopolymers; D014335:Tropomyosin; D014336:Troponin