Protein folding


Ontology type: npg:Subject  | skos:Concept     


Concept Info

NAME

Protein folding

DESCRIPTION

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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Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/ontologies/subjects/protein-folding'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/ontologies/subjects/protein-folding'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/ontologies/subjects/protein-folding'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/ontologies/subjects/protein-folding'


 

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

304 TRIPLES      10 PREDICATES      21 URIs      7 LITERALS

Subject Predicate Object
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14 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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216 sg:ontologies/subjects/protein-design
217 sg:ontologies/subjects/protein-folding
218 sg:ontologies/subjects/protein-function-predictions
219 sg:ontologies/subjects/protein-structure-predictions
220 sg:ontologies/subjects/proteome-informatics
221 sg:ontologies/subjects/quality-control
222 sg:ontologies/subjects/scale-invariance
223 sg:ontologies/subjects/sequence-annotation
224 sg:ontologies/subjects/software
225 sg:ontologies/subjects/standards
226 sg:ontologies/subjects/statistical-methods
227 sg:ontologies/subjects/virtual-drug-screening
228 skos:prefLabel Computational biology and bioinformatics
229 sg:ontologies/subjects/endoplasmic-reticulum sgo:sdDataset onto_subjects
230 rdf:type npg:Subject
231 skos:Concept
232 rdfs:label Endoplasmic reticulum
233 skos:altLabel ER
234 Ergastoplasm
235 skos:broader sg:ontologies/subjects/membrane-trafficking
236 sg:ontologies/subjects/organelles
237 sg:ontologies/subjects/protein-folding
238 skos:definition The endoplasmic reticulum (ER) is a compartment (organelle) in eukaryotic cells that consists of membrane sacs called cisternae. Because of the bound ribosomes, the 'rough' ER is the site of synthesis of various proteins and is where newly synthesized proteins are modified by glycosylation. The 'smooth' ER is a site for lipid and carbohydrate metabolism.
239 skos:inScheme sg:ontologies/subjects/
240 skos:prefLabel Endoplasmic reticulum
241 sg:ontologies/subjects/molecular-biology sgo:sdDataset onto_subjects
242 rdf:type npg:Subject
243 skos:Concept
244 rdfs:label Molecular biology
245 skos:altLabel Biochemical Genetic
246 Biochemical Genetics
247 Molecular Genetic
248 Molecular Genetics
249 skos:broader sg:ontologies/subjects/biological-sciences
250 skos:definition Molecular Biology is the field of biology that studies the composition, structure and interactions of cellular molecules – such as nucleic acids and proteins – that carry out the biological processes essential for the cell’s functions and maintenance.
251 skos:inScheme sg:ontologies/subjects/
252 skos:narrower sg:ontologies/subjects/cell-division
253 sg:ontologies/subjects/chromatin
254 sg:ontologies/subjects/chromosomes
255 sg:ontologies/subjects/crispr-cas-systems
256 sg:ontologies/subjects/dna-damage-and-repair
257 sg:ontologies/subjects/dna-metabolism
258 sg:ontologies/subjects/dna-recombination
259 sg:ontologies/subjects/dna-replication
260 sg:ontologies/subjects/epigenetics
261 sg:ontologies/subjects/non-coding-rnas
262 sg:ontologies/subjects/nuclear-organization
263 sg:ontologies/subjects/post-translational-modifications
264 sg:ontologies/subjects/protein-folding
265 sg:ontologies/subjects/proteolysis
266 sg:ontologies/subjects/proteomics
267 sg:ontologies/subjects/riboswitches
268 sg:ontologies/subjects/ribozymes
269 sg:ontologies/subjects/rna-metabolism
270 sg:ontologies/subjects/rnai
271 sg:ontologies/subjects/single-molecule-biophysics
272 sg:ontologies/subjects/transcription
273 sg:ontologies/subjects/transcriptomics
274 sg:ontologies/subjects/translation
275 sg:ontologies/subjects/transposition
276 skos:prefLabel Molecular biology
277 sg:ontologies/subjects/prions sgo:sdDataset onto_subjects
278 rdf:type npg:Subject
279 skos:Concept
280 rdfs:label Prions
281 skos:altLabel Mink Encephalopathy Virus
282 PrP Proteins
283 Prion Proteins
284 Scrapie
285 Scrapie protein
286 Scrapie proteins
287 skos:broader sg:ontologies/subjects/biochemistry
288 sg:ontologies/subjects/protein-folding
289 skos:definition Prions are an infectious protein usually referring to the protein in mammals called prion (PrP), but the term prions or scrapie protein can be generically applied to any protein that exhibits the same properties of taking on a misfolded conformation (PrPsc form) and templating and propagating further misfolding that leads to its infectivity.
290 skos:inScheme sg:ontologies/subjects/
291 skos:prefLabel Prions
292 sg:ontologies/subjects/protein-aggregation sgo:sdDataset onto_subjects
293 rdf:type npg:Subject
294 skos:Concept
295 rdfs:label Protein aggregation
296 skos:broader sg:ontologies/subjects/protein-folding
297 skos:definition Protein aggregation is the process by which misfolded proteins adopt a conformation that cause its polymerization into aggregates and organized fibrils. Many neurodegenerative diseases (amyloidoses) are associated with protein aggregation, though smaller oligomeric forms of the misfolded (amyloidogenic) proteins have been implicated as the causative agent.
298 skos:inScheme sg:ontologies/subjects/
299 skos:prefLabel Protein aggregation
300 skos:Concept sgo:sdDataset for_codes
301 rdf:type rdfs:Class
302 rdfs:Resource
303 rdfs:subClassOf rdfs:Resource
304 skos:Concept
 




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