Towards symmetry-based explanation of (approximate) shapes of alpha-helices and beta-sheets (and beta-barrels) in protein structure (Q350577): Difference between revisions
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Latest revision as of 15:03, 9 December 2024
scientific article
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English | Towards symmetry-based explanation of (approximate) shapes of alpha-helices and beta-sheets (and beta-barrels) in protein structure |
scientific article |
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Towards symmetry-based explanation of (approximate) shapes of alpha-helices and beta-sheets (and beta-barrels) in protein structure (English)
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9 December 2016
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Summary: 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.
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symmetries
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secondary protein structures
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alpha-helices
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beta-sheets
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beta-barrels
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