Chaperones


Ontology type: npg:Subject  | skos:Concept     


Concept Info

NAME

Chaperones

DESCRIPTION

Chaperones are proteins that assist in protein folding and multi-protein complex assembly co-translationally or post-translationally. Generally, a single chaperone has multiple client proteins. An example of chaperones are heat shock proteins, which are upregulated in response to heat – a risk factor for protein misfolding and aggregation.

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This table displays all metadata directly associated to this object as RDF triples.

104 TRIPLES      9 PREDICATES      13 URIs      6 LITERALS

Subject Predicate Object
1 sg:ontologies/subjects/chaperones sgo:license sg:explorer/license/
2 sgo:sdDataset onto_subjects
3 rdf:type npg:Subject
4 skos:Concept
5 rdfs:label Chaperones
6 skos:altLabel Molecular Chaperone
7 Molecular Chaperones
8 skos:broader sg:ontologies/subjects/protein-folding
9 sg:ontologies/subjects/proteins
10 skos:definition Chaperones are proteins that assist in protein folding and multi-protein complex assembly co-translationally or post-translationally. Generally, a single chaperone has multiple client proteins. An example of chaperones are heat shock proteins, which are upregulated in response to heat – a risk factor for protein misfolding and aggregation.
11 skos:inScheme sg:ontologies/subjects/
12 skos:prefLabel Chaperones
13 sg:ontologies/subjects/ dcterms:description The Nature Subjects Taxonomy is a polyhierarchical categorization of scholarly subject areas which are used for the indexing of content by Springer Nature.
14 dcterms:title Nature Subjects Taxonomy
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26 sg:ontologies/subjects/protein-folding sgo:sdDataset onto_subjects
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38 skos:definition Protein folding is the process by which proteins achieve their mature functional (native) tertiary structure, and often begins co-translationally. Protein folding requires chaperones and often involves stepwise establishment of regular secondary and supersecondary structures, namely α-helices and β-sheets, that fold rapidly, stabilized by hydrogen bonding and disulphide bridges, and then tertiary structure.
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