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Updated: Oct 1, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Gamma-amido-ATP stabilizes a high-fluorescence state of myosin subfragment 1
1Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung, Jahnstr. 29, 69120, Heidelberg, Germany. wray@mpimf-heidelberg.mpg.de
Abstract:
On binding to myosin subfragment 1 (S1), the gamma-amido derivative of ATP (ATPgammaNH2), an isomer of adenosine 5'-[beta,gamma-imido]-triphosphate (AMPPNP), induces a larger increase in the intrinsic (tryptophan) fluorescence than is seen with ATP. A binding constant of 1.7x10(7) M(-1) was measured for ATPgammaNH2, compared to 2.1-2.4x10(7) M(-1) for AMPPNP. ATPgammaNH2 was hydrolyzed only very slowly by S1. ATPgammaNH2 appears to stabilize the 'closed' conformation of S1, and does so without cleavage of the beta-gamma phosphate bond. The dissociation of actin-S1 by ATPgammaNH2 and that of S1.ATPgammaNH2 by actin are both strikingly slow.
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