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Myosin II from rabbit skeletal muscle and Dictyostelium discoideum and its interaction with F-actin studied by (1)H NMR spectroscopy

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Kalbitzer,  Hans Robert
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Kany, H., Wolf, J., & Kalbitzer, H. R. (2002). Myosin II from rabbit skeletal muscle and Dictyostelium discoideum and its interaction with F-actin studied by (1)H NMR spectroscopy. FEBS Letters, 521(1), 121-126. doi:10.1016/S0014-5793(02)02855-7.


Cite as: http://hdl.handle.net/21.11116/0000-0001-EF78-C
Abstract
Mg-F-actin occurs in two conformational states, I and M, where the N-terminal amino acids are either immobile or highly mobile. In the rigor or ADP complex of rabbit myosin S1 with Mg-F-actin the N-terminal acetyl group of actin stays in its highly mobile state. The same is true for the complexes with the myosin motor domain from Dictyostelium discoideum. This excludes a direct strong interaction of the N-terminal amino acids with myosin in the rigor state as suggested. An interaction of the N-terminus of F-actin with myosin is also not promoted by occupying its low-affinity binding site(s) with divalent ions. The N-terminal high-mobility region may be part of a structural system which has evolved for releasing inadequate stress applied to the actin filaments.