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DESCRIBE <http://purl.uniprot.org/SHA-384/E61AD71B15F41D7197F0897DDC1ED16DF95405B7F9ED7E1186635EF0D6FA8AE86F32678D71BB16722E24B0A69C9572C3>
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http://purl.uniprot.org/SHA-384/E61AD71B15F41D7197F0897DDC1ED16DF95405B7F9ED7E1186635EF0D6FA8AE86F32678D71BB16722E24B0A69C9572C3
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/E61AD71B15F41D7197F0897DDC1ED16DF95405B7F9ED7E1186635EF0D6FA8AE86F32678D71BB16722E24B0A69C9572C3
http://www.w3.org/2000/01/rdf-schema#comment
"Results support the global allostery model for hemoglobin A by showing that conformational changes propagate from the effector binding site to the interdimeric interfaces in both quaternary states."
xsd:string
http://purl.uniprot.org/uniprot/#_ECC5A4D77B66D2DE992A3EA89C8BB47EF546370296CD3B38C22EF29F46BF66F511E689381A4571E89481489CB0B79C47
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/E61AD71B15F41D7197F0897DDC1ED16DF95405B7F9ED7E1186635EF0D6FA8AE86F32678D71BB16722E24B0A69C9572C3
http://purl.uniprot.org/uniprot/Q86YQ1
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E61AD71B15F41D7197F0897DDC1ED16DF95405B7F9ED7E1186635EF0D6FA8AE86F32678D71BB16722E24B0A69C9572C3
http://purl.uniprot.org/uniprot/#_Q86YQ1-mappedCitation-16822864
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E61AD71B15F41D7197F0897DDC1ED16DF95405B7F9ED7E1186635EF0D6FA8AE86F32678D71BB16722E24B0A69C9572C3