X-ray diffraction evidence for alpha-helical coiled-coils in native muscle

Cohen, Carolyn; Holmes, Kenneth C.

doi:10.1016/S0022-2836(63)80053-4

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X-ray diffraction evidence for alpha-helical coiled-coils in native muscle

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

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Citation

Cohen, C., & Holmes, K. C. (1963). X-ray diffraction evidence for alpha-helical coiled-coils in native muscle. Journal of Molecular Biology (London), 6(5), 423-432. doi:10.1016/S0022-2836(63)80053-4.

Cite as: https://hdl.handle.net/21.11116/0000-0001-DB6C-0

Abstract

An improved α-diagram has been obtained from a native molluscan “catch” muscle (the anterior byssal retractor muscle of Mytilus edulis). The most striking aspect of the diagram is a strong near-equatorial layer line at about 89 Å. The 5·1 Å spacing is meridional. These features are accounted for by a coiled-coil α-helical structure. Computations indicate that the best fit is obtained with a two-chain structure when various types of disorder are assumed. A possible model is described having a densely packed hydrophobic region between the chains, and most of the polar groups pointing out into the solvent. An implication of the coiled-coil structure is that the α-helix in proteins requires stabilization by side-chain interactions.