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| Evolution of long-range myofibrillar crystallinity in insect flight muscle as examined by X-ray cryomicrodiffraction |
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| Author(s): Iwamoto H, Inoue K, Yagi N |
| Source: PROCEEDINGS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES Volume: 273 Issue: 1587 Pages: 677-685 Published: MAR 22 2006 |
| Times Cited: 6 References: 35 |
| 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 skilful flight has driven the lattice structure towards increased regularity. |
| Document Type: Article |
| Language: English |
| Reprint Address: Iwamoto, H (reprint author), Japan Synchrotron Radiat Res Inst, Res & Utilizat Div, SPring 8, 1-1-1 Kouto, Sayo, Hyogo 6795198 Japan |
Addresses:
1. Japan Synchrotron Radiat Res Inst, Res & Utilizat Div, SPring 8, Sayo, Hyogo 6795198 Japan |
| Publisher: ROYAL SOCIETY, 6-9 CARLTON HOUSE TERRACE, LONDON SW1Y 5AG, ENGLAND |
| Subject Category: Biology; Ecology; Evolutionary Biology |
| IDS Number: 019AC |
| ISSN: 0962-8452 |
| DOI: 10.1098/rspb.2005.3389 |
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