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Identification of the Transitory Complex Myosin-ATP by the Use of α,β-Methylene-ATP

Nature New Biology volume 241, pages 226–229 (1973)Cite this article

Abstract

The normally transitory complex myosin-ATP has been produced as a steady state complex by binding the ATP analogue α,β-methylene-ATP. Studies indicate that its structure is different from that of MADPPi.

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Authors and Affiliations

  1. Max-Planck-Institut für Medizinische Forschung, Heidelberg

    H. G. MANNHERZ, J. BARRINGTON LEIGH, K. C. HOLMES & G. ROSENBAUM

Authors
  1. H. G. MANNHERZ
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  2. J. BARRINGTON LEIGH
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  3. K. C. HOLMES
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  4. G. ROSENBAUM
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MANNHERZ, H., LEIGH, J., HOLMES, K. et al. Identification of the Transitory Complex Myosin-ATP by the Use of α,β-Methylene-ATP. Nature New Biology 241, 226–229 (1973). https://doi.org/10.1038/newbio241226a0

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