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DESCRIBE <http://purl.uniprot.org/SHA-384/40B910336857CF5F42D81D683CFFD26638902C4381BF2F2D4CB7A34FEFA48AF590A7CA344BC98792C0CD0995A32F40F0>
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http://purl.uniprot.org/SHA-384/40B910336857CF5F42D81D683CFFD26638902C4381BF2F2D4CB7A34FEFA48AF590A7CA344BC98792C0CD0995A32F40F0
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/40B910336857CF5F42D81D683CFFD26638902C4381BF2F2D4CB7A34FEFA48AF590A7CA344BC98792C0CD0995A32F40F0
http://www.w3.org/2000/01/rdf-schema#comment
"Both the A-chain and the B-chain of insulin are capable of forming amyloid fibrils in isolation under similar conditions with fibrillar morphologies that differ from those composed of intact insulin."
xsd:string
http://purl.uniprot.org/uniprot/#_A03883FC4E62C4EEE5EC1D56277543C99C66D74EDD342FE144520A6353E56FC3439E5DA4565D3E6E8788385DB0B4E41F
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/40B910336857CF5F42D81D683CFFD26638902C4381BF2F2D4CB7A34FEFA48AF590A7CA344BC98792C0CD0995A32F40F0
http://purl.uniprot.org/uniprot/P01317
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/40B910336857CF5F42D81D683CFFD26638902C4381BF2F2D4CB7A34FEFA48AF590A7CA344BC98792C0CD0995A32F40F0
http://purl.uniprot.org/uniprot/#_P01317-mappedCitation-16774767
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/40B910336857CF5F42D81D683CFFD26638902C4381BF2F2D4CB7A34FEFA48AF590A7CA344BC98792C0CD0995A32F40F0