蛋白质折叠过程中蛋白质骨干和侧链的不同排序,由特定地点的重组红外探测器揭示出来
Sureshbabu Nagarajan1, Humeyra Taskent-Sezgin, Dzmitry Parul
1Department of Chemistry, Emory University, Atlanta, Georgia 30322, USA.
Journal of the American Chemical Society
|November 2, 2011
概括
蛋白质折叠涉及复杂的骨干和侧链排序. 在蛋白质L9折叠中,β-sheet结构中的侧链排序比骨干排序更慢,可能是由于暂时的非原生相互作用.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 蛋白质动力学 蛋白质动力学
背景情况:
- 蛋白质折叠是一个基本的过程,由聚酸骨干和侧链排序之间的相互作用决定.
- 稳定的二次结构的形成,如β-sheet结构,对骨干和侧链排序的相对时间特别敏感.
- 了解这些动态对于破译蛋白质结构-功能关系至关重要.
研究的目的:
- 研究脊柱与侧链在蛋白质L9 (NTL9) N端域折叠期间的时间尺度.
- 开发和应用一种用于特定地点标记和蛋白质动态测量的新方法.
- 阐明过渡性非原生相互作用在蛋白质折叠途径中的作用.
主要方法:
- 使用重组蛋白表达用于特定地点的亚化物 (侧链) 和 (13) C(18) O (脊柱) 红外探测器的结合.
- 采用温度跳跃时间解析的红外光谱学来监测动态.
- 实现了单一残留分辨率,用于独立测量骨干和侧链动态.
主要成果:
- 证明在NTL9的关键β-sheet区域的侧链排序与折叠期间的骨干排序相比,在较慢的时间尺度上发生.
- 确定了一种潜在的机制,涉及暂时形成影响折叠通路的非本土侧链相互作用.
- 验证了一种强大的光谱方法来剖析蛋白质折叠动态.
结论:
- 侧链排序动力学与蛋白质折叠期间的骨干排序动力学不同.
- NTL9的折叠过程涉及复杂的相互作用,侧链相互作用可能落后于脊柱结构形成.
- 这项研究为管理蛋白质折叠的分子机制以及特定相互作用在实现原生结构中的作用提供了新的见解.
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