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• W2163920009 abstract "Insect flight muscle is known for its crystal-quality regularity of contractile protein arrangement within a sarcomere. We have previously shown by X-ray microdiffraction that the crystal-quality regularity in bumble-bee flight muscle is not confined within a sarcomere, but extends over the entire length of a myofibril (>1000 sarcomeres connected in series). Because of this, the whole myofibril may be regarded as a millimetre-long, natural single protein crystal. Using bright X-ray beams from a synchrotron radiation source, we examined how this long-range crystallinity has evolved among winged insects. We analysed >4600 microdiffraction patterns of quick-frozen myofibrils from 50 insect species, covering all the major winged insect orders. The results show that the occurrence of such long-range crystallinity largely coincides with insect orders with asynchronous muscle operation. However, a few of the more skilled fliers among lower-order insects apparently have developed various degrees of structural regularity, suggesting that the demand for skillful flight has driven the lattice structure towards increased regularity." @default.
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• W2163920009 date "2005-12-13" @default.
• W2163920009 modified "2023-09-23" @default.
• W2163920009 title "Evolution of long-range myofibrillar crystallinity in insect flight muscle as examined by X-ray cryomicrodiffraction" @default.
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• W2163920009 doi "https://doi.org/10.1098/rspb.2005.3389" @default.
• W2163920009 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1560076" @default.
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