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http://purl.uniprot.org/citations/10191473http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10191473http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10191473http://www.w3.org/2000/01/rdf-schema#comment"The peptide Val-Arg-Arg-Pro-Asn-Leu-His-Pro-Ser-Phe-Ile-Ala-Ile-Pro-Pro-Lys-Lys-Ile, which corresponds to residues 84-101 of human kappa-casein, has been synthesized and its conformation preferences determined by 1H-nuclear magnetic resonance spectroscopy in dimethyl sulphoxide. The peptide adopted a largely extended chain conformation in solution and there was evidence for the presence of a beta-turn involving residues Pro87-His90 of human kappa-casein. The presence of a turn in this position would make the physiologically significant Arg85 residue of human kappa-casein (which is equivalent to Arg97 in bovine kappa-casein) unavailable for interaction with Asp249 of bovine chymosin, and may partly explain why human kappa-casein is hydrolysed more slowly than its bovine counterpart by bovine chymosin."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.org/dc/terms/identifier"doi:10.1017/s0022029998003318"xsd:string
http://purl.uniprot.org/citations/10191473http://purl.org/dc/terms/identifier"doi:10.1017/s0022029998003318"xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/author"Creamer L.K."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/author"Creamer L.K."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/author"Cross J.J."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/author"Cross J.J."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/author"Liddell M.J."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/author"Liddell M.J."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/author"Plowman J.E."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/author"Plowman J.E."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/name"J. Dairy Res."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/name"J. Dairy Res."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/pages"53-63"xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/pages"53-63"xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/title"Structural features of a peptide corresponding to human kappa-casein residues 84-101 by 1H-nuclear magnetic resonance spectroscopy."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/title"Structural features of a peptide corresponding to human kappa-casein residues 84-101 by 1H-nuclear magnetic resonance spectroscopy."xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/10191473http://purl.uniprot.org/core/volume"66"xsd:string
http://purl.uniprot.org/citations/10191473http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10191473
http://purl.uniprot.org/citations/10191473http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10191473