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¹H, ¹⁵N and ¹³C backbone chemical shift assignment of the titin A67-A68 domain tandem.

作者信息

Czajlik András, Thompson Gary S, Khan Ghulam N, Kalverda Arnout P, Homans Steve W, Trinick John

机构信息

Institute for Molecular and Cellular Biology and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.

出版信息

Biomol NMR Assign. 2012 Apr;6(1):39-41. doi: 10.1007/s12104-011-9321-6. Epub 2011 Jul 21.

DOI:10.1007/s12104-011-9321-6
PMID:21779926
Abstract

Single molecules of the giant protein titin extend across half of the muscle sarcomere, from the Z-line to the M-line, and have roles in muscle assembly and elasticity. In the A-band titin is attached to thick filaments and here the domain arrangement occurs in regular patterns of eleven called the large super-repeat. The large super-repeat itself occurs eleven times and forms nearly half the titin molecule. Interactions of the large super-repeats with myosin are consistent with a role in thick filament assembly. Here we report backbone assignments of the titin A67-A68 domain tandem (Fn-Ig) from the third super-repeat (A65-A75) completed using triple resonance NMR experiments.

摘要

相似文献

1
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2
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引用本文的文献

1
¹H, ¹⁵N, and ¹³C backbone chemical shift assignment of titin domains A59-A60 and A60 alone.肌联蛋白A59 - A60结构域及单独的A60结构域的¹H、¹⁵N和¹³C主链化学位移归属
Biomol NMR Assign. 2014 Oct;8(2):429-33. doi: 10.1007/s12104-013-9532-0. Epub 2014 Jan 28.