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

Mannherz, Hans Georg; Barrington Leigh, John; Holmes, Kenneth C.; Rosenbaum, Gerd

doi:10.1038/newbio241226a0

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

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Mannherz, Hans Georg
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Holmes, Kenneth C.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Mannherz, H. G., Barrington Leigh, J., Holmes, K. C., & Rosenbaum, G. (1973). Identification of the Transitory Complex Myosin-ATP by the Use of α,β-Methylene-ATP. Nature New Biology, 241, 226-229. doi:10.1038/newbio241226a0.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-B18E-0

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.