通过串行同步晶体学捕获的细菌素中的质子吸收机制
Tobias Weinert1, Petr Skopintsev2, Daniel James2
1Division of Biology and Chemistry-Laboratory for Biomolecular Research, Paul Scherrer Institut, 5232 Villigen, Switzerland. tobias.weinert@psi.ch.
研究人员使用同步晶体学可视化了蛋白质动态,捕获了bacteriorhodopsin
科学领域:
- 结构生物学
- 生物物理
- 蛋白质动力学
背景情况:
- 蛋白质的结构动力学对于生物功能至关重要.
- 想象这些快速的运动需要先进的结构技术.
研究的目的:
- 适应时间分辨率串行晶体学对同步子源.
- 为了可视化bacteriorhodopsin的功能构造变化.
- 在200毫秒的时间范围内捕捉蛋白质的运动.
主要方法:
- 适用于同步 X 射线源的时间解析串行晶体学.
- 细菌素的光激活.
- 数据收集和分析随着时间的推移而发生的结构变化.
主要成果:
- 在光激活后的前5毫秒内观察到细菌素的结构变化,与X射线激光数据相似.
- 在10-15毫秒之间检测到细胞质侧显著的结构重组 (高达9安格斯特罗姆).
- 确定了特定残留物的旋转 (白氨酸-93,氨酸-219) 打开了一条通道,形成了质子转移的水链.
结论:
- 基于同步子的时间解析串行晶体学对于研究蛋白质动态是有效的.
- 解释了细菌素光循环中的关键结构事件,包括质子释放和随后的充电.
- 揭示了质子线形成的机制, 对于质子的功能至关重要.
更多相关视频
10:45Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021
09:09Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography
Published on: September 20, 2016
相关概念视频
X-ray Crystallography
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
Serial Position Effect
Proton (¹H) NMR: Chemical Shift
Absorption signals of all the protium nuclei...
¹H NMR of Labile Protons: Temporal Resolution
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
¹H NMR of Labile Protons: Deuterium (²H) Substitution
Drugs Affecting Neurotransmitter Release or Uptake
