The Journal of cell biology, 138(3), 559-574 (1997-08-11)
The effect of the type of metal ion (i.e., Ca2+, Mg2+, or none) bound to the high-affinity divalent cation binding site (HAS) of actin on filament assembly, structure, and dynamics was investigated in the absence and presence of the mushroom
We have used thiol cross-linking and electron paramagnetic resonance (EPR) to resolve structural transitions of myosin's light chain domain (LCD) and catalytic domain (CD) that are associated with force generation. Spin labels were incorporated into the LCD of muscle fibers
Rate constants for the reactions of Cys-697 and Cys-707 of skeletal muscle myosin subfragment 1 (S1) with N,N'-p-phenylenedimaleimide (pPDM) and its monofunctional analog phenylmaleimide (PM) were measured for S1 and S1 bound to nucleotides and/or actin. The [pPDM] and [PM]
Journal of molecular biology, 387(4), 869-882 (2009-04-03)
The mechanism of salt-induced actin polymerization involves the energetically unfavorable nucleation step, followed by filament elongation by the addition of monomers. The use of a bifunctional cross-linker, N,N'-(1,4-phenylene)dimaleimide, revealed rapid formation of the so-called lower dimers (LD) in which actin
The Biochemical journal, 450(1), 23-35 (2012-12-06)
In the present paper, we described our attempt to characterize the rough three-dimensional features of the structural analogue of the key intermediate of myosin's cross-bridge cycle. Using quick-freeze deep-etch replica electron microscopy, we observed that actin-attached myosin during in vitro
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