Gauge symmetries and structure of proteins

Abstract

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.

arXiv comment8 pages, 5 figures. Prepared for the proceedings of the XII Quark Confinement and the Hadron Spectrum, 29 August to 3 September 2016, Thessaloniki, Greece

References in corpus (6)

• The Discrete Frenet Frame, Inflection Point Solitons And Curve Visualization with Applications to Folded Proteins
• Topological Solitons and Folded Proteins
• A Gauge Field Theory of Chirally Folded Homopolymers with Applications to Folded Proteins
• Gauge field, strings, solitons, anomalies and the speed of life
• Thermal unfolding of myoglobin in the Landau-Ginzburg-Wilson approach
• On the role of thermal backbone fluctuations in myoglobin ligand gate dynamics

Cited by in corpus (4)

• An introduction to kinks in ${\phi }^4$-theory
• Leading Quantum Correction to the ${\Phi }^4$ Kink Form Factor
• Emergence of oscillons in kink-impurity interactions
• Chern-Simons-Higgs Model as a Theory of Protein Molecules