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The Discrete Frenet Frame, Inflection Point Solitons And Curve Visualization with Applications to Folded Proteins

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arxiv 1102.5658 v1 pith:3XZFG5M3 submitted 2011-02-28 q-bio.BM cond-mat.softhep-thphysics.bio-ph

classification q-bio.BMcond-mat.softhep-thphysics.bio-ph
keywords discretecurvesframingfrenetproteinsalongapproachbackbone
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abstract

We develop a transfer matrix formalism to visualize the framing of discrete piecewise linear curves in three dimensional space. Our approach is based on the concept of an intrinsically discrete curve, which enables us to more effectively describe curves that in the limit where the length of line segments vanishes approach fractal structures in lieu of continuous curves. We verify that in the case of differentiable curves the continuum limit of our discrete equation does reproduce the generalized Frenet equation. As an application we consider folded proteins, their Hausdorff dimension is known to be fractal. We explain how to employ the orientation of $C_\beta$ carbons of amino acids along a protein backbone to introduce a preferred framing along the backbone. By analyzing the experimentally resolved fold geometries in the Protein Data Bank we observe that this $C_\beta$ framing relates intimately to the discrete Frenet framing. We also explain how inflection points can be located in the loops, and clarify their distinctive r\^ole in determining the loop structure of foldel proteins.

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Cited by 2 Pith papers

Reviewed papers in the Pith corpus that reference this work. Sorted by Pith novelty score. Full citation record

  1. A Continuous Effective Model of the Protein Dynamics

    q-bio.BM 2019-08 reject novelty 5.0 of 10

    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.

  2. Chern-Simons-Higgs Model as a Theory of Protein Molecules

    cond-mat.soft 2019-08 conditional novelty 4.0 of 10

    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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