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      Three-dimensional structure of myosin subfragment-1: a molecular motor.

      Science (New York, N.Y.)
      Actins, metabolism, Adenosine Triphosphate, Amino Acid Sequence, Binding Sites, Crystallization, Image Processing, Computer-Assisted, Methylation, Models, Molecular, Molecular Sequence Data, Muscle Contraction, Myosin Subfragments, chemistry, Protein Conformation, Protein Structure, Secondary, X-Ray Diffraction

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          Abstract

          Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.

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