k Computer generated spacefilling model showing ten actin monomers from an Factin helix, a polymer of the protein actin. For clarity each actin monomer the repeated polymer unit is shown in a different colour. Each aminoacid residue is represented by a sphere of radius 2.7 angstroms. In muscle cells, actin forms part of the thin filament, which cyclically interacts with the thick myosin filament to produce a mutual sliding that is the basis of muscle contraction. The white spheres are aminoacid residues that crosslink to the myosin in the actomyosin complex. The structure of the Factin filament was determined using a technique called Xray fibre diffraction. Editorial Stock Photo - Afloimages
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Computer generated space-filling model showing ten actin monomers from an F-actin helix, a polymer of the protein actin. For clarity each actin monomer (the repeated polymer unit) is shown in a different colour. Each amino-acid residue is represented by a sphere of radius 2.7 angstroms. In muscle cells, actin forms part of the thin filament, which cyclically interacts with the thick myosin filament to produce a mutual sliding that is the basis of muscle contraction. The white spheres are amino-acid residues that cross-link to the myosin in the actomyosin complex. The structure of the F-actin filament was determined using a technique called X-ray fibre diffraction.
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Computer generated space-filling model showing ten actin monomers from an F-actin helix, a polymer of the protein actin. For clarity each actin monomer (the repeated polymer unit) is shown in a different colour. Each amino-acid residue is represented by a sphere of radius 2.7 angstroms. In muscle cells, actin forms part of the thin filament, which cyclically interacts with the thick myosin filament to produce a mutual sliding that is the basis of muscle contraction. The white spheres are amino-acid residues that cross-link to the myosin in the actomyosin complex. The structure of the F-actin filament was determined using a technique called X-ray fibre diffraction.

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10571406

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Editorial

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Creation date
15-11-2010

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