A Conformational Change in F-Actin When Myosin Binds: Fluorescence Resonance Energy Transfer Detects an Increase in the Radial Coordinate of Cys-374
Author:
Affiliation:
1. Muscle Research Unit, Department of Anatomy and Histology, Institute for Biomedical Research, The University of Sydney, Sydney 2006, Australia
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi962588l
Reference44 articles.
1. The Environment of the High-Affinity Cation Binding Site on Actin and the Separation between Cation and ATP Sites as Revealed by Proton NMR and Fluorescence Spectroscopy1
2. Fluorescence resonance energy transfer between sites in G-actin. The spatial relationship between Cys-10, Tyr-69, Cys-374, the high-affinity metal and the nucleotide
3. Kinetics of Association of Myosin Subfragment-1 to Unlabeled and Pyrenyl-labeled Actin
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