Conformational changes of troponin C within the thin filaments detected by neutron scattering

Matsumoto, Fumiko*; Makino, Koji*; Maeda, Kayo*; Patzelt, H.*; Maeda, Yuichiro*; Fujiwara, Satoru

Journal of Molecular Biology, 342(4), p.1209 - 1221, 2004/09

https://doi.org/10.1016/j.jmb.2004.07.086

Regulation of skeletal and cardiac muscle contraction is associated with the thin filament-based proteins, troponin C (TnC), TnI, TnT, tropomyosin, and actin. Knowledge of structures of these proteins is indispensable for elucidating the molecular mechanism of this Ca-sensitive regulation. Here the structure of TnC within the thin filaments was investigated with neutron scattering, combined with selective deuteration and the contrast matching technique. Deuterated TnC was prepared, reconstituted into the native thin filaments, and neutron scattering patterns of these reconstituted thin filaments containing deuterated TnC were measured under the condition where non-deuterated components were rendered 'invisible' to neutrons. The obtained scattering curves arising only from deuterated TnC were analyzed by model calculations using the Monte Carlo method. The results showed that upon binding of Ca, radius of gyration of TnC changed from 23 AA to 24 AA , and the radial position of TnC within the thin filament changed from 53 AA to 49 AA .