Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.
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Linear dichroism of acrylodan-labeled tropomyosin and myosin subfragment 1 bound to actin in myofibrils.Polarization of fluorescently labeled myosin subfragment-1 fully or partially decorating muscle fibers and myofibrils.Fluorescence polarization of skeletal muscle fibers labeled with rhodamine isomers on the myosin heavy chain.Paramagnetic probes attached to a light chain on the myosin head are highly disordered in active muscle fibers.Form birefringence of muscle.Orientation of spin-labeled light chain-2 exchanged onto myosin cross-bridges in glycerinated muscle fibers.Muscle cross-bridges bound to actin are disordered in the presence of 2,3-butanedione monoxime.Luminescence resonance energy transfer measurements in myosin.Steady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethylrhodamine.Model-independent electron spin resonance for measuring order of immobile components in a biological assembly.Single-headed binding of a spin-labeled-HMM-ADP complex to F-actin. Saturation transfer electron paramagnetic resonance and sedimentation studiesTheory of sample translation in fluorescence correlation spectroscopy.Effect of ATP depletion on the isolated thick filament of limulus striated muscle.Effect of negative mechanical stress on the orientation of myosin cross-bridges in muscle fibers.Effect of planar dielectric interfaces on fluorescence emission and detection. Evanescent excitation with high-aperture collection.Order in supported phospholipid monolayers detected by the dichroism of fluorescence excited with polarized evanescent illumination.Evidence for pre- and post-power stroke of cross-bridges of contracting skeletal myofibrils.In situ fluorescent protein imaging with metal film-enhanced total internal reflection microscopy.Orientation of DNA in agarose gels.Effect of a myosin regulatory light chain mutation K104E on actin-myosin interactions.GFP-tagged regulatory light chain monitors single myosin lever-arm orientation in a muscle fiber.Calculation of the polarized fluorescence from a labeled muscle fiber.On the mechanism of energy transduction in myosin subfragment 1.Fraction of myosin cross-bridges bound to actin in active muscle fibers: estimation by fluorescence anisotropy measurements.Myosin cross-bridge orientation in rigor and in the presence of nucleotide studied by electron spin resonance.Time-resolved fluorescence polarization from ordered biological assembliesOrientation of spin-labeled nucleotides bound to myosin in glycerinated muscle fibers.Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscleOrientation changes in myosin regulatory light chains following photorelease of ATP in skinned muscle fibers
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P2860
Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1983
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.
@en
Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.
@nl
type
label
Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.
@en
Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.
@nl
prefLabel
Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.
@en
Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.
@nl
P2093
P2860
P356
P1476
Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.
@en
P2093
P2860
P304
P356
10.1073/PNAS.80.24.7515
P407
P577
1983-12-01T00:00:00Z