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Hemoglobin Rothschild: Structural Rationalization of Decreased O <sub>2</sub> Affinity as a Consequence of a β37(C3)Trp→Arg Mutation

2024-06-06

Abstract excerpt

Hemoglobin Rothschild is characterized by a β37(C3)Trp→Arg mutation that severely impairs wildtype hemoglobin function. This mutation has previously been documented to diminish conformational cooperativity, and thereby uppercut oxygen affinity. While the mutation is known to have direct implications on the hinge region at the α 1 β 2 interface, the immediate and indirect manifestations of this mutation have not b...

Identifiers and source

Literature Corpus work
8ae6feda-ad1d-598d-9f76-db6fd8cd87f0
DOI
10.1101/2024.06.06.597804
Open publication

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Hemoglobin Rothschild: Structural Rationalization of Decreased O <sub>2</sub> Affinity as a Consequence of a β37(C3)Trp→Arg MutationDOI 10.1101/2024.06.06.597804
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