Fluorescent-Probe Studies of Contractile Proteins

Robert A. Mendelson
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Robert A. Mendelson: University of California, Department of Biochemistry and Biophysics and The Cardiovascular Research Institute

Chapter 19 in Cell and Muscle Motility, 1982, pp 257-278 from Springer

Abstract: Abstract The present knowledge of the mechanism of muscle contraction and cell movement at the molecular level comes from an accumulation of experimental evidence obtained using a wide variety of biochemical and biophysical techniques. In relatively recent times, the use of intrinsic and extrinsic fluorescence probes has provided useful information about the kinetic intermediates, mobility, binding, orientation, intramolecular distances, and site environment of the globular head region of the myosin molecule, both free in solution and as a part of the intact muscle “cross-bridges” that are thought to be the impellers of biological movement.

Keywords: Fluorescence Polarization; Contractile Protein; Sarcomere Length; Myosin Head; Thick Filament (search for similar items in EconPapers)
Date: 1982
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DOI: 10.1007/978-1-4684-4037-9_19

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