在蛋白质崩中剖析卷和缺乏溶剂效应
Frauke Gräter1, Pascal Heider, Ronen Zangi
1Department of Chemistry, Columbia University, 3000 Broadway, New York, New York 10027, USA. frauke@picb.ac.cn
Journal of the American Chemical Society
|August 13, 2008
概括
蛋白质弹性指导折叠. 水中的疏水力显著地软化了蛋白质,减少了脊柱的硬性,并使其能够超出简单的卷积,从而解释了实验观察.
科学领域:
- 生物物理学的生物物理.
- 分子生物学分子生物学
- 计算化学计算化学
背景情况:
- 蛋白质折叠和崩是受蛋白质弹性引导的早期事件.
- 在蛋白质弹性反应中,热力和水力作用的作用尚未完全理解.
研究的目的:
- 调查卷和疏水力对蛋白质弹性的贡献.
- 使用分子模拟,将蛋白质的弹性行为与链模型进行比较.
主要方法:
- 利用分子模拟来研究伸展的ubiquitin.
- 将模拟结果与蛋白质作为链模型进行比较.
- 分析了疏水力对蛋白质持久性长度的影响.
主要成果:
- 发现了蛋白质骨干的高内在刚度,其持久长度为1.2nm.
- 证明,疏水力显著降低了这种刚性,使其明显持久长度为0.3-0.6nm.
- 在恶劣的溶剂条件下 (水) 观测到超出热线圈的蛋白质紧缩.
结论:
- 疏水力在确定水溶液中蛋白质表面弹性的过程中起着至关重要的作用.
- 在单分子实验中观察到的蛋白质柔软性主要是由于水中的疏水性相互作用.
- 溶剂环境显著影响蛋白质紧缩和弹性特性.
相关概念视频
Protein Folding
Overview
Protein Folding
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...
Protein Folding
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Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
Molecular Chaperones and Protein Folding
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
Protein and Protein Structure
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
A protein's shape is critical to its function. For example, an enzyme can...


