S. Harvey, H. Cheung, K. Thames
Mar 1, 1977
Citations
1
Influential Citations
22
Citations
Quality indicators
Journal
Archives of biochemistry and biophysics
Abstract
Abstract The fluorescence lifetime of 1, N 6 -ethenoadenosine diphosphate (ϵ-ADP) is 33 ns when bound to F-actin at 4 °C. When heavy meromyosin or myosin subfragment-1 binds to the F-actin filament, the lifetime of ϵ-ADP drops, reaching 29 ns when every actin monomer is bound to a myosin head. The change in lifetime is a consequence of cooperative conformational changes among the actin monomers. The results of these experiments support the contention that there are differences in the ways in which the two heads of the myosin molecule interact with the actin filament.