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Gauge symmetries and structure of proteins
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We discuss the gauge field theory approach to protein structure study, which allows a natural way to introduce collective degrees of freedom and nonlinear topological structures. Local symmetry of proteins and its breaking in the medium is considered, what allows to derive Abelian Higgs model of protein backbone, correct folding of which is defined by gauge symmetry breaking due hydrophobic forces. Within this model structure of protein backbone is defined by superposition of one-dimensional topological solitons (kinks), what allows to reproduce the three-dimensional structure of the protein backbone with precision up to 1A and to predict its dynamics.
Forward citations
Cited by 2 Pith papers
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A Continuous Effective Model of the Protein Dynamics
A continuous field theory model predicts that protein beta strands have a universal length of about 12 Å, with their abundance controlled by a single parameter.
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Chern-Simons-Higgs Model as a Theory of Protein Molecules
A four-parameter Chern-Simons-Higgs model fits the curvature-torsion relation of protein secondary structure, with one remaining parameter controlling loop length and strand abundance.
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