相关实验视频

Updated: Jul 16, 2025

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

从冷电磁图像的统计数据中确定子单元-子单元相互作用:在昼夜钟蛋白质复合体中观察近邻合

Xu Han¹, Dongliang Zhang¹, Lu Hong²

¹State Key Laboratory of Artificial Microstructure and Mesoscopic Physics, School of Physics, Peking University, Beijing, 100871, China.

Nature communications

|September 22, 2023

概括

研究人员开发了一种研究分子复合物的新方法,揭示了蓝藻细菌中的KaiC蛋白如何改变其结构. 这为生物过程调节和蛋白质动态提供了洞察力.

科学领域:

结构生物学是结构生物学.
生物物理学的生物物理.
生物化学生化学

背景情况:

生物功能依赖于复杂的分子机器.
直接测量这些复合体内的子单元相互作用是具有挑战性的.
菌中的KaiC蛋白质是昼夜时钟的关键组成部分.

研究的目的:

开发一种分析分子复合体中子单元相互作用的一般方法.
为了研究KaiC六合体的构造状态和动态.
了解酸化如何影响KaiC六合体形状和合作性.

主要方法:

结合低温电子显微镜 (cryo-EM) 与统计建模.
聚集了数以百万计的KaiC单体图像以识别构造状态.
根据不同的子单位安排,分类了超过16万个KaiC六合体.
应用了伊辛格模型来定量地适应六边形形状图案.

主要成果:

鉴定了单个KaiC单体的两个主要构造状态.
在KaiC六合环中发现了13种单体状态的独特空间安排.
在六合体中,邻近的子单位之间展示了显著的合作关系.
表明酸化会改变子单元构成概率.

结论:

KaiC 六合体对酸化水平的变化表现出类似开关的反应.
开发的方法为研究动态分子复合体提供了一种强大的方法.
这些发现有助于更好地理解昼夜时钟机制和蛋白质的合作性.

更多相关视频

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE

Published on: May 16, 2017

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

相关概念视频

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...