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A Gauge Field Theory of Chirally Folded Homopolymers with Applications to Folded Proteins
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We combine the principle of gauge invariance with extrinsic string geometry to develop a lattice model that can be employed to theoretically describe properties of chiral, unbranched homopolymers. We find that in its low temperature phase the model is in the same universality class with proteins that are deposited in the Protein Data Bank, in the sense of the compactness index. We apply the model to analyze various statistical aspects of folded proteins. Curiously we find that it can produce results that are a very good good match to the data in the Protein Data Bank.
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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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