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The Structure and Topology of α-Helical Coiled Coils

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cris.lastimport.scopus2024-02-12T20:51:26Z
dc.abstract.en$α$-Helical coiled coils constitute one of the most diverse folds yet described. They range in length over two orders of magnitude; they form rods, segmented ropes, barrels, funnels, sheets, spirals, and rings, which encompass anywhere from two to more than 20 helices in parallel or antiparallel orientation; they assume different helix crossing angles, degrees of supercoiling, and packing geometries. This structural diversity supports a wide range of biological functions, allowing them to form mechanically rigid structures, provide levers for molecular motors, project domains across large distances, mediate oligomerization, transduce conformational changes and facilitate the transport of other molecules. Unlike almost any other protein fold known to us, their structure can be computed from parametric equations, making them an ideal model system for rational protein design. Here we outline the principles by which coiled coils are structured, review the determinants of their folding and stability, and present an overview of their diverse architectures.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorDunin-Horkawicz, Stanisław
dc.contributor.authorBassler, Jens
dc.contributor.authorLupas, Andrei N.
dc.date.accessioned2024-01-28T12:03:17Z
dc.date.available2024-01-28T12:03:17Z
dc.date.issued2017
dc.description.financeNie dotyczy
dc.identifier.doi10.1007/978-3-319-49674-0_4
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/137528
dc.pbn.affiliationbiological sciences
dc.publisher.ministerialSpringer
dc.relation.bookFibrous proteins : structures and mechanisms
dc.rightsClosedAccess
dc.sciencecloudnosend
dc.titleThe Structure and Topology of α-Helical Coiled Coils
dc.typeMonographChapter
dspace.entity.typePublication