固态 NMR 证据表明蜘蛛拖丝中存在弹性蛋白样β-转角结构。
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
机构信息
Department of Chemistry and Biochemistry, Magnetic Resonance Research Center, Arizona State University, Tempe, AZ 85287, USA.
出版信息
Chem Commun (Camb). 2010 Sep 28;46(36):6714-6. doi: 10.1039/c0cc00829j. Epub 2010 Aug 23.
PMID:20733981
Abstract
Two-dimensional homo- and heteronuclear solid-state MAS NMR experiments on (13)C/(15)N-proline labeled Argiope aurantia dragline silk provide evidence for an elastin-like beta-turn structure for the repetitive Gly-Pro-Gly-X-X motif prevalent in major ampullate spidroin 2 (MaSp2).
摘要
（13）C/（15）N-脯氨酸标记的金蛛牵丝氨酸的二维同核和异核固态 MAS NMR 实验为富含在主要壶腹丝蛋白 2（MaSp2）中的重复 Gly-Pro-Gly-X-X 基序的弹性蛋白样β-转角结构提供了证据。
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