Refine your search:     
Report No.

Internal dynamics of F-actin and myosin subfragment-1 studied by quasielastic neutron scattering

Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Nakajima, Kenji  ; Kawamura, Seiko; Kikuchi, Tatsuya; Fujiwara, Satoru

Various biological functions related to cell motility are driven by the interaction between the partner proteins, actin and myosin. To obtain insights into how this interaction occurs, the internal dynamics of F-actin and myosin subfragment-1 (S1) were characterized by quasielastic neutron scattering measurements on the solution samples of F-actin and S1. Contributions of the internal motions of the proteins to the scattering spectra were separated from those of the global macromolecular diffusion. Analysis of the spectra arising from the internal dynamics showed that the correlation times of the atomic motions were about two times shorter for F-actin than for S1, suggesting that F-actin fluctuates more rapidly than S1. It was also shown that the fraction of the immobile atoms is larger for S1 than for F-actin. These results suggest that F-actin actively facilitates the binding of myosin by utilizing the more frequent conformational fluctuations than those of S1.



- Accesses




Category:Biochemistry & Molecular Biology



[CLARIVATE ANALYTICS], [WEB OF SCIENCE], [HIGHLY CITED PAPER & CUP LOGO] and [HOT PAPER & FIRE LOGO] are trademarks of Clarivate Analytics, and/or its affiliated company or companies, and used herein by permission and/or license.