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Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
蛋白质折叠的尺寸和序列以及体积变化
Jean-Baptiste Rouget1, Tural Aksel, Julien Roche
1Centre de Biochimie Structurale, INSERM U1054, CNRS UMR5048, Université Montpellier 1, Montpellier, France.
Journal of the American Chemical Society
|March 31, 2011
概括
液压压力导致蛋白质展开,因为在折叠状态下内部包装不完美,而不是均的水分效应. 这种局部的包装缺陷揭示了蛋白质结构合作性和稳定性的洞察力.
科学领域:
- 生物物理学的生物物理.
- 结构生物学 结构生物学
- 蛋白质科学 蛋白质科学
背景情况:
- 水静压通常会诱导蛋白质展开.
- 勒查特利尔原理表明,展开的状态具有较小的摩尔体积.
- 在蛋白质展开时体积变化 (ΔV(u)) 的具体起源仍然不清楚.
研究的目的:
- 研究影响蛋白质展开时体积变化的因素 (ΔV(u)).
- 为了确定蛋白质大小和序列对ΔV (u) 的贡献.
- 阐明压力对蛋白质影响的结构基础.
主要方法:
- 利用了诺奇受体林重复域的删除变体的模型系统.
- 系统地检查了蛋白质大小和序列对 ΔV 的影响.
- 分析了蛋白质结构中包装缺陷的局部性质.
主要成果:
- 提供了强有力的证据,证明在折叠状态下不完美的内部包装是对蛋白质压力影响的主要原因.
- 确定了包装缺陷,这些缺陷位于3D蛋白质结构中.
- 证明了蛋白质构成能量调节体积特性,影响稳定性.
结论:
- 不完善的内部蛋白质包装是压力诱导展开的主要原因.
- 局部的包装缺陷,而不是均的水分,驱动压力效应.
- 这项研究提供了关于蛋白质合作性,长距离合和稳定性的见解.
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
Overview
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...

