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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Evolution of the Potential Energy Landscape with Static Pulling Force for Two Model Proteins
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Evolution of the Potential Energy Landscape with Static Pulling Force for Two Model Proteins

机译:两种模型蛋白质在静态拉力作用下的势能态演化

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摘要

The energy landscape is analyzed for off-lattice bead models of protein L and protein G as a function of a static pulling force. Two different pairs of attachment points (pulling directions) are compared in each case, namely, residues 1/56 and 10/32. For the terminal residue pulUng direction 1/56, the distinct global minimum structures are all extended, aside from the compact geometry that correlates with zero force. The helical turns finally disappear at the highest pulling forces considered. For the 10/32 pulling direction, the changes are more complicated, with a variety of competing arrangements for beads outside the region where the force is directly applied. These alternatives produce frustrated energy landscapes, with low-lying minima separated by high barriers. The calculated folding pathways in the absence of force are in good agreement with previous work. The N-terminal hairpin folds first for protein L and the C-terminal hairpin for protein G, which exhibits an intermediate. However, for a relatively low static force, where the global minimum retains its structure, the folding mechanisms change, sometimes dramatically, depending on the protein and the attachment points. The scaling relations predicted by catastrophe theory are found to hold in the limit of short path lengths.
机译:针对静态拉力的函数,分析了蛋白质L和蛋白质G的非晶格珠模型的能量分布。分别比较两对不同的附着点(牵引方向),即残基1/56和10/32。对于末端残渣推动方向1/56,除了与零力相关的紧凑几何形状以外,所有其他全局最小结构都得到扩展。在所考虑的最大拉力下,螺旋转弯最终消失了。对于10/32的拉动方向,变化更加复杂,在直接施加力的区域之外,珠子有多种竞争性布置。这些替代方案产生了令人沮丧的能源格局,低洼的极小点被高壁垒隔开。在没有力的情况下计算出的折叠路径与先前的工作非常吻合。 N末端发夹先折叠后出现蛋白L,C末端发夹先折叠后出现蛋白G。但是,对于相对较低的静态力(整体最小值保留其结构),折叠机制有时会发生很大变化,具体取决于蛋白质和附着点。发现由突变理论预测的比例关系保持在短路径长度的限制内。

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