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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Property / DOI: 10.3390/sym4010015 / rank | |||
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Property / author: Vladik Ya. Kreinovich / rank | |||
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Property / author: Vladik Ya. Kreinovich / rank | |||
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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. | |||
Property / review text: 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. / rank | |||
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Property / Mathematics Subject Classification ID: 92D20 / rank | |||
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Property / Mathematics Subject Classification ID: 22E70 / rank | |||
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Property / Mathematics Subject Classification ID: 54H15 / rank | |||
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Property / Mathematics Subject Classification ID: 57S99 / rank | |||
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Property / zbMATH DE Number: 6662241 / rank | |||
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symmetries | |||
Property / zbMATH Keywords: symmetries / rank | |||
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secondary protein structures | |||
Property / zbMATH Keywords: secondary protein structures / rank | |||
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alpha-helices | |||
Property / zbMATH Keywords: alpha-helices / rank | |||
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beta-sheets | |||
Property / zbMATH Keywords: beta-sheets / rank | |||
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beta-barrels | |||
Property / zbMATH Keywords: beta-barrels / rank | |||
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Property / MaRDI profile type: MaRDI publication profile / rank | |||
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Property / full work available at URL: https://doi.org/10.3390/sym4010015 / rank | |||
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Property / OpenAlex ID: W2124109894 / rank | |||
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Property / DOI: 10.3390/SYM4010015 / rank | |||
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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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