Internal motions of actin characterized by quasielastic neutron scattering

中性子準弾性散乱によるアクチン内部運動の特徴づけ

藤原 悟; Plazanet, M.*; 松本 富美子; 小田 俊郎*

Fujiwara, Satoru; Plazanet, M.*; Matsumoto, Fumiko; Oda, Toshiro*

The quasielastic neutron scattering (QENS) experiments were carried out to characterize the internal dynamics of the protein, actin in the polymerized form (F-actin) and the monomeric form (G-actin). To investigate the effects of hydration, the measurements were done on the powder samples containing only the first layer of hydration water, and those containing more layers of water. The QENS spectra obtained indicated that the internal motions of both F-actin and G-actin have distributions of motions with distinct correlation times and amplitudes. Increasing hydration changes relative populations of these distinct motions. The effects of hydration were shown to be different between F-actin and G-actin. The elastic incoherent neutron scattering measurements provided the concerted results. The observed effects were interpreted in terms of the differences in the dynamical heterogeneity of G-actin and F-actin.