在β-桶蛋白周围映射水化动态
Jin Yang1, Yafang Wang1, Lijuan Wang1
1Department of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.
Journal of the American Chemical Society
|March 2, 2017
概括
蛋白质水化动态在阿尔法螺旋和β叶蛋白之间是异质的. 液化水的动态比蛋白质的放松更快,影响蛋白质的波动和二次结构之间的差异.
科学领域:
- 生物物理
- 结构生物学
- 蛋白质动力学
背景情况:
- 蛋白质表面的水分对于蛋白质的结构,灵活性,动态和功能至关重要.
- 了解蛋白质结构与水分动态之间的关系是一项挑战.
研究的目的:
- 系统地描述围绕贝塔桶蛋白的水合动态,鼠肝脂肪酸结合蛋白 (rLFABP).
- 揭示不同蛋白质二次结构 (beta-sheet与alpha-helical) 对水行为的影响.
主要方法:
- 在蛋白质表面使用基扫描, 检查17个不同的位置.
- 使用超快速光谱观察水合水放松和托芬侧链异性变异的动态.
主要成果:
- 观察到三种不同的补水放松时间尺度 (数百 femtosecond 到数百 picosecond).
- 确定了两种不同的托芬侧链放松时间尺度 (几十到几百小秒).
- 发现的水化动态是异质的,外层水的放松速度更快 (数百 femtosecond) 和内层水的放松速度在皮秒到百皮秒的时间尺度上.
结论:
- 液化动态比蛋白质放松更快,并驱动皮秒级蛋白质波动.
- 与阿尔法螺旋形图案相比,水化动态在贝塔板结构周围通常较慢.
- 比起α螺旋蛋白,β片蛋白具有更厚的水化外和更硬的界面水化网络.
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