Towards symmetry-based explanation of (approximate) shapes of alpha-helices and beta-sheets (and beta-barrels) in protein structure (Q350577): Difference between revisions

From MaRDI portal
Importer (talk | contribs)
Created a new Item
 
Importer (talk | contribs)
Changed an Item
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.
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
 
Normal rank
Property / Mathematics Subject Classification ID
 
Property / Mathematics Subject Classification ID: 92D20 / rank
 
Normal rank
Property / Mathematics Subject Classification ID
 
Property / Mathematics Subject Classification ID: 22E70 / rank
 
Normal rank
Property / Mathematics Subject Classification ID
 
Property / Mathematics Subject Classification ID: 54H15 / rank
 
Normal rank
Property / Mathematics Subject Classification ID
 
Property / Mathematics Subject Classification ID: 57S99 / rank
 
Normal rank
Property / zbMATH DE Number
 
Property / zbMATH DE Number: 6662241 / rank
 
Normal rank
Property / zbMATH Keywords
 
symmetries
Property / zbMATH Keywords: symmetries / rank
 
Normal rank
Property / zbMATH Keywords
 
secondary protein structures
Property / zbMATH Keywords: secondary protein structures / rank
 
Normal rank
Property / zbMATH Keywords
 
alpha-helices
Property / zbMATH Keywords: alpha-helices / rank
 
Normal rank
Property / zbMATH Keywords
 
beta-sheets
Property / zbMATH Keywords: beta-sheets / rank
 
Normal rank
Property / zbMATH Keywords
 
beta-barrels
Property / zbMATH Keywords: beta-barrels / rank
 
Normal rank

Revision as of 08:17, 28 June 2023

scientific article
Language Label Description Also known as
English
Towards symmetry-based explanation of (approximate) shapes of alpha-helices and beta-sheets (and beta-barrels) in protein structure
scientific article

    Statements

    Towards symmetry-based explanation of (approximate) shapes of alpha-helices and beta-sheets (and beta-barrels) in protein structure (English)
    0 references
    0 references
    0 references
    0 references
    9 December 2016
    0 references
    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.
    0 references
    symmetries
    0 references
    secondary protein structures
    0 references
    alpha-helices
    0 references
    beta-sheets
    0 references
    beta-barrels
    0 references

    Identifiers

    0 references
    0 references
    0 references
    0 references
    0 references
    0 references