Solid-state NMR structure determination of whole anchoring threads from the blue mussel Mytilus edulis.

Solid-state NMR structure determination of whole anchoring threads from the blue mussel Mytilus edulis.
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蓝贻贝整个锚固线的固态核磁共振结构测定。

DOI:
10.1021/bm301493u
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发表时间:
2013
期刊:
影响因子:
6.2
通讯作者:
I. Marcotte
I. Marcotte
中科院分区:
化学2区
文献类型:
--
作者:
A. Arnold;F. Byette;Marc;André Leblanc;L. Sleno;R. Tremblay;C. Pellerin;I. Marcotte

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利用全标记纤维的二维(13)C固体核磁共振研究了紫贻贝(Mytilus edulis)整条锚定丝的分子结构。这种独特的材料被证明在分子水平上是有序的,尽管它的非均匀组成,如低于1.5 ppm的窄线宽所证明的。光谱主要由胶原环境中的残基,从化学位移分析确定,和一个完整的二维分配(包括次要氨基酸)是可能的。对于扭转角(-75°,+150°)的胶原螺旋,预测和实验主链化学位移之间的最佳一致性。丰富的甘氨酸和丙氨酸残基可以在多达五种不同的结构环境中解析。丙氨酸峰可归属于胶原蛋白三螺旋、β-折叠(平行和反平行)、β-转角和无序结构。ATR-FTIR显微镜的使用证实了这些结构环境的存在,并使它们能够定位在线的核心(胶原螺旋和反平行β-片层)或其角质层(无序结构)中。该方法应该能够在分子水平上表征大范围的足丝宏观性质。
The molecular structure of the blue mussel Mytilus edulis whole anchoring threads was studied by two-dimensional (13)C solid-state NMR on fully labeled fibers. This unique material proves to be well ordered at a molecular level despite its heterogeneous composition as evidenced by the narrow measured linewidths below 1.5 ppm. The spectra are dominated by residues in collagen environments, as determined from chemical shift analysis, and a complete two-dimensional assignment (including minor amino acids) was possible. The best agreement between predicted and experimental backbone chemical shifts was obtained for collagen helices with torsion angles (-75°, +150°). The abundant glycine and alanine residues can be resolved in up to five different structural environments. Alanine peaks could be assigned to collagen triple-helices, β-sheets (parallel and antiparallel), β-turns, and unordered structures. The use of ATR-FTIR microscopy confirmed the presence of these structural environments and enabled their location in the core of the thread (collagen helices and antiparallel β-sheets) or its cuticle (unordered structures). The approach should enable characterization at the molecular level of a wide range of byssus macroscopic properties.
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