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Symmetry 2012, 4(1), 15-25; doi:10.3390/sym4010015

Towards Symmetry-Based Explanation of (Approximate) Shapes of Alpha-Helices and Beta-Sheets (and Beta-Barrels) in Protein Structure

Department of Computer Science, University of Texas at El Paso, 500 West University Avenue, El Paso, TX 79968, USA
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Received: 22 December 2011 / Revised: 6 January 2012 / Accepted: 12 January 2012 / Published: 19 January 2012
(This article belongs to the Special Issue Symmetry Group Methods for Molecular Systems)
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Abstract

Protein structure is invariably connected to protein function. There are two important secondary structure elements: alpha-helices and beta-sheets (which sometimes come in a shape of beta-barrels). The actual shapes of these structures can be complicated, but in the first approximation, they are usually approximated by, correspondingly, cylindrical spirals and planes (and cylinders, for beta-barrels). In this paper, following the ideas pioneered by a renowned mathematician M. Gromov, we use natural symmetries to show that, under reasonable assumptions, these geometric shapes are indeed the best approximating families for secondary structures.
Keywords: symmetries; secondary protein structures; alpha-helices; beta-sheets; beta-barrels symmetries; secondary protein structures; alpha-helices; beta-sheets; beta-barrels
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Nava, J.; Kreinovich, V. Towards Symmetry-Based Explanation of (Approximate) Shapes of Alpha-Helices and Beta-Sheets (and Beta-Barrels) in Protein Structure. Symmetry 2012, 4, 15-25.

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