Observation of two orientations from rigor cross-bridges in glycerinated muscle fibers
- 7 October 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (20) , 6203-6207
- https://doi.org/10.1021/bi00368a055
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 24 references indexed in Scilit:
- Model-independent time-resolved fluorescence depolarization from ordered biological assemblies applied to restricted motion of myosin cross-bridges in muscle fibersBiochemistry, 1986
- Characterization of the isolated 20 kDa and 50 kDa fragments of the myosin headBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Crosslinking of actin to myosin subfragment 1: course of reaction and stoichiometry of productsBiochemistry, 1985
- Crossbridge order and orientation in resting single glycerinated muscle fibres studied by linear dichroism of bound rhodamine labelsJournal of Muscle Research and Cell Motility, 1984
- Model-Independent fluorescence polarization for measuring order in a biological assemblyBiopolymers, 1984
- Three-dimensional reconstruction of rigor insect flight muscle from tilted thin sectionsNature, 1984
- Cross-bridge orientation in skeletal muscle measured by linear dichroism of an extrinsic chromophoreJournal of Molecular Biology, 1982
- Energetics and kinetics of the interconversion of two myosin subfragment-1.cntdot.adenosine 5'-diphosphate complexes as viewed by phosphorus-31 nuclear magnetic resonanceBiochemistry, 1981
- Angles of nucleotides bound to cross-bridges in glycerinated muscle fiber at various concentrations of ϵ-ATP, ϵ-ADP and ϵ-AMPPNP detected by polarized fluorescenceJournal of Molecular Biology, 1981
- Coupling between the enzymatic site of myosin and the mechanical output of muscleJournal of Molecular Biology, 1979