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- W2078244199 abstract "We have studied the solution structure of skeletal muscle troponin C complexed with troponin I in the presence of calcium using small-angle X-ray and neutron scattering. 4Ca2+.troponin C in the complex has an extended dumbbell shape with a radius of gyration of 23.9 +/- 0.5 A and a maximum linear dimension of approximately 72 A, similar to the values obtained from the crystal structure coordinates of troponin C (Herzberg & James, 1985). Troponin I is even more extended than troponin C with a radius of gyration of 41 +/- 2 A and a maximum linear dimension of approximately 118 A. The centers-of-mass for each component of the complex are approximately coincident (< 10-A separation) as are their long axes, and the troponin I component encompasses the 4Ca2+.troponin C. These data provide new insights into the nature of the conformational arrangement of this important Ca(2+)-sensitive molecular switch." @default.
- W2078244199 created "2016-06-24" @default.
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- W2078244199 date "1994-07-01" @default.
- W2078244199 modified "2023-10-13" @default.
- W2078244199 title "Troponin I Encompasses an Extended Troponin C in the Ca2+-Bound Complex: A Small-Angle X-ray and Neutron Scattering Study" @default.
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- W2078244199 doi "https://doi.org/10.1021/bi00193a009" @default.
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