相关实验视频
Updated: May 25, 2025
12:42
Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
15.0K
异常的依赖力过渡速率揭示了亚-协酶A结合蛋白的折叠和展开动态中的双重路径
Yuhang Zhang1,2, Zhuwei Zhang1,2, Hao Sun2
1Research Institute for Biomimetics and Soft Matter, Fujian Provincial Key Lab for Soft Functional Materials Research, Department of Physics, Xiamen University, Xiamen 361005, China.
The journal of physical chemistry letters
|February 28, 2025
概括
乙-协酶A结合蛋白 (ACBP) 呈现出异常的依赖力折叠和展开速度. 拉伸力可以在两个不同的过渡路径之间切换,揭示了全α蛋白质中复杂的强力反应行为.
科学领域:
- 生物物理学的生物物理.
- 蛋白质动力学 蛋白质动力学
- 分子力光谱学 分子力光谱学
背景情况:
- 所有α蛋白,如乙-协酶A结合蛋白 (ACBP),以快速折叠和低机械稳定性而闻名.
- 以往使用生物化学和单分子力光谱对ACBP折叠路径和过渡状态构造的研究已经产生了相互矛盾的结果.
- 了解ACBP的机械特性对于描述全α蛋白超级家族的折叠动态至关重要.
研究的目的:
- 调查ACBP在不同机械力 (4-10 pN) 下的折叠和展开动态.
- 为了解决围绕ACBP折叠路径和过渡状态构成的争议.
- 阐明ACBP中异常的依赖力过渡速率背后的机制.
主要方法:
- 使用磁子来对ACBP施加受控的力.
- 在4-10 pN的力范围内测量了折叠和展开的速度.
- 进行了与分子动力学模拟相结合的详细分析.
主要成果:
- 观察到异常的依赖力过渡速率:展开速率在6 pN以下保持不变,在6 pN以上急剧增加.
- 证明折叠率的对数几乎是施加力的线性函数.
- 确定了ACBP的两个不同的过渡途径:一个在低力时占主导地位,另一个在高力时占主导地位.
结论:
- 拉伸力显著调节ACBP的折叠和展开速度.
- 施加的力作为一个开关,改变主导的过渡路径.
- 由于强力诱导的路径切换,ACBP表现出复杂的强力反应行为,为蛋白质力学提供了新的见解.
相关概念视频
01:58Cooperative Allosteric Transitions
2.3K
2.3K
01:25Protein Folding
7.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
7.7K
03:00Molecular Chaperones and Protein Folding
12.9K
12.9K
01:16Protein-Drug Binding: Mechanism and Kinetics
240
Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
240
01:13Induced-fit Model
80.1K
Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
80.1K
01:19Enzyme Kinetics
95.6K
Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
95.6K