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• W1981869745 abstract "A recently developed approach for mapping protein-domain orientations in the cellular environment was used to investigate the Ca2+-dependent structural changes in the tropomyosin/troponin complex on the actin filament that regulate muscle contraction. Polarized fluorescence from bifunctional rhodamine probes attached along four α helices of troponin C (TnC) was measured in permeabilized skeletal muscle fibers. In relaxed muscle, the N-terminal lobe of TnC is less closed than in crystal structures of the Ca2+-free domain, and its D helix is approximately perpendicular to the actin filament. In contrast to crystal structures of isolated TnC, the D and E helices are not collinear. On muscle activation, the N lobe orientation becomes more disordered and the average angle between the C helix and the filament changes by 32° ± 5°. These results illustrate the potential of in situ measurements of helix and domain orientations for elucidating structure-function relations in native macromolecular complexes. A recently developed approach for mapping protein-domain orientations in the cellular environment was used to investigate the Ca2+-dependent structural changes in the tropomyosin/troponin complex on the actin filament that regulate muscle contraction. Polarized fluorescence from bifunctional rhodamine probes attached along four α helices of troponin C (TnC) was measured in permeabilized skeletal muscle fibers. In relaxed muscle, the N-terminal lobe of TnC is less closed than in crystal structures of the Ca2+-free domain, and its D helix is approximately perpendicular to the actin filament. In contrast to crystal structures of isolated TnC, the D and E helices are not collinear. On muscle activation, the N lobe orientation becomes more disordered and the average angle between the C helix and the filament changes by 32° ± 5°. These results illustrate the potential of in situ measurements of helix and domain orientations for elucidating structure-function relations in native macromolecular complexes." @default.
• W1981869745 created "2016-06-24" @default.
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• W1981869745 date "2003-04-01" @default.
• W1981869745 modified "2023-10-17" @default.
• W1981869745 title "In Situ Orientations of Protein Domains" @default.
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• W1981869745 doi "https://doi.org/10.1016/s1097-2765(03)00096-0" @default.
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