Chern-Simons-Higgs model as a theory of protein molecules

被引:3
作者
Melnikov, Dmitry [1 ,2 ]
Neves, Alyson B. F. [3 ,4 ]
机构
[1] Univ Fed Rio Grande do Norte, Int Inst Phys, Campus Univ, BR-59078970 Natal, RN, Brazil
[2] Inst Theoret & Expt Phys, B Cheremushkinskaya 25, Moscow 117218, Russia
[3] Univ Fed Rio Grande do Norte, Dept Theoret & Expt Phys, Campus Univ, BR-59078970 Natal, RN, Brazil
[4] Univ Fed Maranhao, Campus Balsas,Rua Jose Leao 484, BR-65800000 Balsas, Maranhao, Brazil
基金
俄罗斯科学基金会;
关键词
POLYPEPTIDE; GEOMETRY; DYNAMICS; LINKING; NUMBER;
D O I
10.1063/1.5137808
中图分类号
O59 [应用物理学];
学科分类号
摘要
In this paper, we discuss a one-dimensional Abelian-Higgs model with Chern-Simons interaction as an effective theory of one-dimensional curves embedded in a three-dimensional space. We demonstrate how this effective model is compatible with the geometry of protein molecules. Using standard field theory techniques, we analyze phenomenologically interesting static configurations of the model and discuss their stability. This simple model predicts some characteristic relations for the geometry of secondary structure motifs of proteins, and we show how this is consistent with the experimental data. After using the data to universally fix basic local geometric parameters, such as the curvature and torsion of the helical motifs, we are left with a single free parameter. We explain how this parameter controls the abundance and shape of the principal motifs (alpha helices, beta strands, and loops connecting them).
引用
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页数:22
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