Next Article in Journal
Symmetries of Spatial Graphs and Rational Twists along Spheres and Tori
Previous Article in Journal
Convex-Faced Combinatorially Regular Polyhedra of Small Genus
Open AccessArticle

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
*
Author to whom correspondence should be addressed.
Symmetry 2012, 4(1), 15-25; https://doi.org/10.3390/sym4010015
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)
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. View Full-Text
Keywords: symmetries; secondary protein structures; alpha-helices; beta-sheets; beta-barrels symmetries; secondary protein structures; alpha-helices; beta-sheets; beta-barrels
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.

Show more citation formats Show less citations formats

Article Access Map by Country/Region

1
Only visits after 24 November 2015 are recorded.
Back to TopTop