相关实验视频

Updated: Jan 17, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

在体内交联质谱:解码蛋白质构造动态和复杂的调节网络在活细胞的进步和挑战

Jing Chen¹, Qun Zhao², Yukui Zhang²

¹State Key Laboratory of Medical Proteomics, National Chromatographic R. & A. Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China; University of Science and Technology of China, Hefei 230026, China.

Current opinion in chemical biology

|September 13, 2025

概括

在体内化学交联质谱 (XL-MS) 绘制活细胞中的蛋白质结构和相互作用. 最近的进展增强了它分析生物分子功能和网络的能力.

科学领域:

生物化学生物化学
蛋白质组学是指蛋白质组学.
结构生物学结构生物学

背景情况:

在体内化学交联质谱 (XL-MS) 对于绘制活细胞内的蛋白质结构和相互作用至关重要.
它提供了距离约束,以在生理条件下表征蛋白质构造和相互作用网络.
在系统层面上,XL-MS有助于理解生物宏分子功能和调节机制.

研究的目的:

系统地审查最近在体内XL-MS.的进步.
突出该技术在蛋白质构成和相互作用网络分析方面的优势.
讨论当前的挑战和该领域的未来方向.

主要方法:

对交叉链接器设计和交叉链接丰富的近期进展的审查.
对XL-MS的质谱学和人工智能辅助数据分析方面的进展进行分析.
专注于高通量,在体内对蛋白质复合体进行全蛋白质组范围的映射.

主要成果:

由于技术改进,体内XL-MS能力的显著扩展.
在识别交叉连接和确定距离约束时提高精度.
增加了用于分析蛋白质动态的时空分辨率.

结论:

在体内XL-MS是一种强大而不断发展的技术,用于研究蛋白质结构和相互作用.
持续的进步有望更深入地了解细胞机制.
解决当前的技术挑战将进一步释放XL-MS的潜力.

更多相关视频

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Covalent Labeling with Diethylpyrocarbonate for Studying Protein Higher-Order Structure by Mass Spectrometry

Covalent Labeling with Diethylpyrocarbonate for Studying Protein Higher-Order Structure by Mass Spectrometry

Published on: June 15, 2021

相关概念视频

Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...