超快速的交换揭示了在细胞染色体c折叠的初始阶段发生的特定结构事件
Hossein Fazelinia1, Ming Xu, Hong Cheng
1Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, United States.
Journal of the American Chemical Society
|December 25, 2013
概括
马细胞染色体c中的早期蛋白质折叠是由α-螺旋段内的特定相互作用驱动的,而不是一般的疏水性崩. 这项微流体增强的NMR研究揭示了蛋白质折叠动态的早期结构偏好.
科学领域:
- 蛋白质折叠的动态 蛋白质折叠的动态
- 生物物理化学 生物物理化学
- 结构生物学是结构生物学.
背景情况:
- 蛋白质在速度限制步骤之前,在早期折叠阶段经常显著紧.
- 这种初始紧缩背后的驱动力 (特定相互作用与疏水性崩) 仍在争论中.
研究的目的:
- 阐明驱动初始蛋白质链凝结的机制.
- 在早期蛋白质折叠中区分特定的折叠事件和一般的疏水性崩.
主要方法:
- 利用微流体来实现NMR检测的H/D交换标签的微秒时间分辨率.
- 在马细胞染色体c折叠的最初140微秒内,监测了50多个骨干NH组的键形成.
- 分析了H/D交换和折叠之间的竞争,以及展开的国家汇率.
主要成果:
- 在两个C端α螺旋段中观察到溶剂屏蔽的胺质子集群.
- 发现N端螺旋在早期折叠阶段基本上没有结构.
- 主要结构中指示的接近性促进了早期的螺旋形成和结合.
结论:
- 马细胞染色体c中的初始链凝结是由α-螺旋段之间的特定相互作用驱动的.
- 研究结果驳斥了一般的疏水性崩作为早期紧缩的主要驱动因素.
- 在较后的折叠阶段,N端和C端螺旋之间形成长距离接触.
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