Abstract
When Galvani discovered the electrical regulation of muscle contraction science began an inexorable transformation. Observation of an inorganic trigger for a physiological event presaged the end of vitalism, the beginning of electrochemistry, and over 400 years of research into the first demonstrable biochemical machine: striated muscle. This molecular machine has been studied in various contexts, ranging from holistic (live muscle) to reductionist (purified molecules). Generations of scientists have, collectively, disassembled and reassembled the contractile apparatus of striated muscle, demonstrating an increasingly complete understanding of its function. In the process, high resolution structuresa have been determined for most components of this machine. Given the relative orientation of these proteins in a muscle fiber, visualization of muscle contraction at the atomic level seems attainable. This effort is complicated by the inherent properties of proteins, specifically, proteins with conformationally heterogeneous native ensembles.
Here “structure” or “structural” refers to models of protein tertiary or quaternary structure. “Resolution” originates in the context of scattering methods (optics and diffraction), but is also used to refer to the “spatial precision of coordinates” in the context of structural models.
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Hoffman, R.M.B., Sykes, B.D. (2007). Disposition and Dynamics: Interdomain Orientations in Troponin. In: Ebashi, S., Ohtsuki, I. (eds) Regulatory Mechanisms of Striated Muscle Contraction. Advances in Experimental Medicine and Biology, vol 592. Springer, Tokyo. https://doi.org/10.1007/978-4-431-38453-3_7
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DOI: https://doi.org/10.1007/978-4-431-38453-3_7
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