Influence of fluctuations in actin structure on myosin V step size.
We study the influence of helical disorder in the actin structure on the myosin V step size, predicted from the elastic lever arm model. We show that fluctuations of +/-5 degrees per actin subunit, as proposed by Egelman et al., significantly alter the distribution of step sizes and improve the agreement with experimental data.
Vilfan
Andrej
A
J. Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia. andrej.vilfran@ijs.si
D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000465:Algorithms; D004548:Elasticity; D004735:Energy Transfer; D006868:Hydrolysis; D008958:Models, Molecular; D015233:Models, Statistical; D024701:Myosin Type V / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation
D000199:Actins; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D024701:Myosin Type V