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http://purl.uniprot.org/SHA-384/1A6D447D37B9452C0D9D2B5C4FE248841F1E8234FB4C7DCDB8CB1C7AA21FD0802D5342CFABE9992C97DB5A1AF84A8BDFhttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/1A6D447D37B9452C0D9D2B5C4FE248841F1E8234FB4C7DCDB8CB1C7AA21FD0802D5342CFABE9992C97DB5A1AF84A8BDFhttp://www.w3.org/2000/01/rdf-schema#comment"Data suggest that the stronger effect of K72A mutation on the peroxidase activity of human versus yeast cytochrome c results from relief of steric interactions between side chains at positions 72 and 81 (Ile in human vs Ala in yeast) which suppresses the dynamics of omega-loop D necessary for the intrinsic peroxidase activity of cytochrome c."xsd:string
http://purl.uniprot.org/uniprot/#_AD56CF4CF6B62AD20F0A9D276845E33FC8E7366C1D744C8DE310AD0B1B6712588A97AD681C52B8F899E36B0EDF004FE4http://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/1A6D447D37B9452C0D9D2B5C4FE248841F1E8234FB4C7DCDB8CB1C7AA21FD0802D5342CFABE9992C97DB5A1AF84A8BDF
http://purl.uniprot.org/uniprot/P99999http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/1A6D447D37B9452C0D9D2B5C4FE248841F1E8234FB4C7DCDB8CB1C7AA21FD0802D5342CFABE9992C97DB5A1AF84A8BDF
http://purl.uniprot.org/uniprot/#_P99999-mappedCitation-28598148http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/1A6D447D37B9452C0D9D2B5C4FE248841F1E8234FB4C7DCDB8CB1C7AA21FD0802D5342CFABE9992C97DB5A1AF84A8BDF