对于由平行和元动力学相结合而产生的β毛针折叠的自由能量景观
Giovanni Bussi1, Francesco Luigi Gervasio, Alessandro Laio
1Computational Science, Department of Chemistry and Applied Biosciences, Eidgenössische Technische Hochschule Zürich, c/o USI Campus, Via Buffi 13, CH-6900 Lugano, Switzerland. gbussi@ethz.ch
Journal of the American Chemical Society
|October 13, 2006
概括
我们通过结合并行和元动力学来开发了一种新的自由能量计算方法. 这种方法增强了高自由能量区域的采样,用于在显式水中进行β发针折叠.
科学领域:
- 计算化学计算化学
- 生物物理学的生物物理.
- 分子动力学分子动力学
背景情况:
- 了解蛋白质折叠动态对于分子生物学来说至关重要.
- 自由能量计算对于描述蛋白质构成状态至关重要.
- 模拟像β毛针折叠这样的复杂系统需要先进的计算方法.
研究的目的:
- 开发和验证一种新的,增强的自由能量计算方法.
- 为了研究白色水中的β毛针折叠的自由能量景观.
- 提高抽样高自由能源地区的效率.
主要方法:
- 联合并行和元动力学 (PT-MetaD).
- 适用于在明确水中对β毛针折叠的应用.
- 分析自由能量盆地和形态状态.
主要成果:
- PT-MetaD方法显著优于传统的并行和元动力学.
- 成功取样了以前无法进入的高自由能量的区域.
- 折叠和展开状态之间的量化和差异.
- 在自由能量盆地内特征的主导配置.
结论:
- 新的PT-MetaD方法为自由能量计算提供了一种强大的方法.
- 这种方法提高了蛋白质折叠景观的准确表征.
- 提供了对折叠蛋白质的热力学和结构组合的见解.
相关概念视频
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 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
Protein Folding
Overview
Gibbs Free Energy
One of the challenges of using the second law of thermodynamics to determine if a process is spontaneous is that it requires measurements of the entropy change for the system and the entropy change for the surroundings. An alternative approach involving a new thermodynamic property defined in terms of system properties only was introduced in the late nineteenth century by American mathematician Josiah Willard Gibbs. This new property is called the Gibbs free energy (G) (or simply the free...
Arrhenius Plots
The Arrhenius equation relates the activation energy and the rate constant, k, for chemical reactions. In the Arrhenius equation, k = Ae−Ea/RT, R is the ideal gas constant, which has a value of 8.314 J/mol·K, T is the temperature on the kelvin scale, Ea is the activation energy in J/mole, e is the constant 2.7183, and A is a constant called the frequency factor, which is related to the frequency of collisions and the orientation of the reacting molecules.
The Arrhenius equation can be used to...
The Arrhenius equation can be used to...


