摘要: THE tropomyosin molecule consists of two α helices, which form a coiled-coil little over 400 A long1. Besides forming crystals, can be precipitated with divalent cations to produce needle shaped aggregates (showing variety patterns cross striations in the electron microscope2) for detailed molecular packings have not been established. At low resolution, however, helices may regarded as smooth rods. The structure such could depend, some extent, on considerations closest packing This possibility seems first considered by Rudall3 his discussion crystal protein from Mantis egg case, where he showed that double close-packed sheets staggering each helix one quarter pitch respect next. I report here idea stagger between molecules, conjunction certain microscope results, leads value helix.
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