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Topological Solitons and Folded Proteins

Abstract : We propose that protein loops can be interpreted as topological domain-wall solitons. They interpolate between ground states that are the secondary structures like alpha-helices and beta-strands. Entire proteins can then be folded simply by assembling the solitons together, one after another. We present a simple theoretical model that realizes our proposal and apply it to a number of biologically active proteins including 1VII, 2RB8, 3EBX (Protein Data Bank codes). In all the examples that we have considered we are able to construct solitons that reproduce secondary structural motifs such as alpha-helix-loop-alpha-helix and beta-sheet-loop-beta-sheet with an overall root-mean-square-distance accuracy of around 0.7 Angstrom or less for the central alpha-carbons, i.e. within the limits of current experimental accuracy.
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https://hal.archives-ouvertes.fr/hal-00466540
Contributor : Maxim Chernodub <>
Submitted on : Wednesday, March 24, 2010 - 10:19:29 AM
Last modification on : Tuesday, April 21, 2020 - 10:29:58 AM

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M. N. Chernodub, Shuangwei Hu, Antti J. Niemi. Topological Solitons and Folded Proteins. Physical Review E : Statistical, Nonlinear, and Soft Matter Physics, American Physical Society, 2010, 82 (1), pp.011916. ⟨10.1103/PhysRevE.82.011916⟩. ⟨hal-00466540⟩

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