φ4相互作用引起的构象变化和蛋白质折叠

Mariska Januar, A. Sulaiman, L. T. Handoko
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引用次数: 3

摘要

提出了一种基于拉格朗日方法并施加一定对称性破缺的蛋白质构象动力学模型。蛋白质和注入的非线性源的构象变化都用玻色子拉格朗日量表示,源的相互作用为\phi^4。在该模型中,表示内部氢键的蛋白质的弹簧张力被实现为单个氨基酸与非线性源之间的相互作用。折叠途径是由通过蛋白质主干传播的非线性源的强度决定的。结果表明,该模型与前人的一些研究结果相吻合。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Conformation changes and protein folding induced by φ4 interaction
A model to describe the mechanism of conformational dynamics in protein based on matter interactions using lagrangian approach and imposing certain symmetry breaking is proposed. Both conformation changes of proteins and the injected non-linear sources are represented by the bosonic lagrangian with an additional \phi^4 interaction for the sources. In the model the spring tension of protein representing the internal hydrogen bonds is realized as the interactions between individual amino acids and nonlinear sources. The folding pathway is determined by the strength of nonlinear sources that propagate through the protein backbone. It is also shown that the model reproduces the results in some previous works.
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