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摘要翻译：
提出了一个基于物质相互作用的蛋白质构象动力学模型，该模型采用拉格朗日方法，并施加一定的对称性破缺。蛋白质和注入的非线性源的构象变化都用波速拉格朗日方程来表示，并对源有附加的π4相互作用。在该模型中，表达蛋白质内部氢键的弹簧张力被理解为单个氨基酸与非线性源的相互作用。折叠途径是由非线性源的强度，传播通过蛋白质主链。该模型重现了前人一些工作中的结果。
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英文标题：
《Conformation changes and protein folding induced by \phi^4 interaction》
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作者：
M. Januar, A. Sulaiman, L.T. Handoko
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最新提交年份：
2011
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分类信息：
一级分类：Physics 物理学
二级分类：Biological Physics 生物物理学
分类描述：Molecular biophysics, cellular biophysics, neurological biophysics, membrane biophysics, single-molecule biophysics, ecological biophysics, quantum phenomena in biological systems (quantum biophysics), theoretical biophysics, molecular dynamics/modeling and simulation, game theory, biomechanics, bioinformatics, microorganisms, virology, evolution, biophysical methods.
分子生物物理、细胞生物物理、神经生物物理、膜生物物理、单分子生物物理、生态生物物理、生物系统中的量子现象（量子生物物理）、理论生物物理、分子动力学/建模与模拟、博弈论、生物力学、生物信息学、微生物、病毒学、进化论、生物物理方法。
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一级分类：Quantitative Biology 数量生物学
二级分类：Other Quantitative Biology 其他定量生物学
分类描述：Work in quantitative biology that does not fit into the other q-bio classifications
不适合其他q-bio分类的定量生物学工作
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英文摘要：
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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PDF链接：
https://arxiv.org/pdf/1109.6065
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