About: The Structure and Topology of α-Helical Coiled Coils

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	The Structure and Topology of α-Helical Coiled Coils
Creator	Lupas, Andrei Bassler, J Bassler, Jens Dunin-Horkawicz, S Dunin-Horkawicz, Stanislaw Lupas, A
source	Medline; PMC
abstract	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.
has issue date	2017-01-19(xsd:dateTime)
bibo:doi	10.1007/978-3-319-49674-0_4
bibo:pmid	28101860
has license	no-cc
sha1sum (hex)	7c2c5321f0aa4ae1e7f6c1a1dcbdadef085a87e5
schema:url	https://doi.org/10.1007/978-3-319-49674-0_4
resource representing a document's title	The Structure and Topology of α-Helical Coiled Coils
has PubMed Central identifier	PMC7122542
has PubMed identifier	28101860
schema:publication	Fibrous Proteins: Structures and Mechanisms
resource representing a document's body	covid:7c2c5321f0aa4ae1e7f6c1a1dcbdadef085a87e5#body_text
is schema:about of	named entity 'oligomerization' named entity 'project' named entity 'This' named entity 'helix' named entity 'supercoiling' named entity 'KNOWN' named entity 'DISTANCES' named entity 'STRUCTURE' named entity 'DIFFERENT' named entity 'MEDIATE' named entity 'SHEETS' named entity 'ALMOST' named entity 'BIOLOGICAL FUNCTIONS' named entity 'MAGNITUDE' named entity 'FOLDS' named entity 'TRANSPORT' named entity 'DESCRIBED' named entity 'HELICES' named entity 'PROVIDE' named entity 'SEGMENTED ' named entity 'FORM' named entity 'RANGE' named entity 'PARALLEL' named entity 'CROSSING' named entity 'STRUCTURES' named entity 'GEOMETRIES' named entity 'MORE THAN' named entity 'DIVERSITY' named entity 'TOPOLOGY' named entity 'COILS' named entity 'OLIGOMERIZATION' named entity 'RINGS' named entity 'COILS' named entity 'HELICAL' named entity 'HELICAL' named entity 'COILED' named entity 'ALLOWING' named entity 'SPIRALS' named entity 'CHANGES' named entity 'LENGTH' named entity 'ONE OF' named entity 'COILED' named entity 'COMPUTED' named entity 'ORIENTATION' named entity 'RIGID' named entity 'DEGREES' named entity 'THEIR' named entity 'WIDE' named entity 'STRUCTURAL' named entity 'HELIX' named entity 'DIVERSE' named entity 'PROTEIN FOLD' named entity 'LARGE' named entity 'TO FORM' named entity 'RODS' named entity 'ORDERS' named entity 'PACKING' named entity 'ANGLES' named entity 'MOLECULES' named entity 'STRUCTURE' named entity 'ACROSS' named entity 'MOLECULAR MOTORS' named entity 'PROJECT' named entity 'wide range' named entity 'rings' named entity 'orders' named entity 'parametric' named entity 'protein fold' named entity 'rigid' named entity 'helix' named entity 'antiparallel' named entity 'protein fold' named entity 'transduce' named entity 'superhelical' named entity 'phenylalanine' named entity 'bacteriophage'

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