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蜘蛛丝蛋白的自我组装是由一个pH值敏感的继电器控制的
Glareh Askarieh1, My Hedhammar, Kerstin Nordling
1Department of Chemistry, Oslo University, 1033 Blindern, 0315 Oslo, Norway.
Nature
|May 14, 2010
概括
蜘蛛丝蛋白,spidroins,被存储在一个流体状态. 蜘蛛的氨基末端域 (NT) 控制了自我组装,防止过早的聚合,并使丝形成.
科学领域:
- 生物化学 生物化学
- 材料科学 材料科学 材料科学
- 结构生物学 结构生物学
背景情况:
- 蜘蛛丝是一种高性能生物聚合物,由蜘蛛制成,作为液体物储存.
- 蜘蛛具有重复的细分和保存的非重复域,这对丝特性至关重要.
- 在自组装之前防止过早聚合的机制仍然不清楚.
研究的目的:
- 研究氨基终端域 (NT) 在蜘蛛自我组装和聚合中的作用.
- 阐明蜘蛛储存和丝形成的分子细节.
- 了解蜘蛛如何在生产丝时控制蛋白质聚合.
主要方法:
- 进行X射线晶体学以确定NT域的结构.
- 工程迷你蜘蛛体内纳入NT领域.
- 评估不同pH值的工程蜘蛛的自我组装和聚合特性.
主要成果:
- NT域形成了一个具有独特结构的反平行五螺旋捆的同位体.
- 将NT纳入迷你螺旋使得pH值依赖于pH值6.3左右的自组装成为可能.
- 在中性pH (7以上) 时,NT会延迟聚合,而在较低pH时会加速聚合.
结论:
- NT 域起到分子开关的作用,调节蜘蛛组合.
- 涉及NT的类似继电器的机制控制了储存和挤出过程中的蜘蛛聚合.
- NT的二维结构和电荷分布很可能在蜘蛛中保持.
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