Abstract
A new haemoglobin variant with a decreased oxygen affinity is described, in which the substitution, alpha 94 (G1) Asp replaced by Asn, affects the alpha1beta2 contact alpha1G1-beta2G4. The relevance of this variant to our understanding of the importance of the hydrogen bond between alpha1G1 and beta2G4 in Perutz's model of oxyhaemoglobin A is discussed.
MeSH terms
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Asparagine / analysis
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Aspartic Acid / analysis
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Binding Sites
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Child, Preschool
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Female
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Hemoglobins
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Hemoglobins, Abnormal*
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Humans
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Kansas
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Kinetics
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Macromolecular Substances
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Oxygen / blood*
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Peptide Fragments / analysis
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Phytic Acid / blood
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Protein Binding
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Texas
Substances
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Hemoglobins
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Hemoglobins, Abnormal
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Macromolecular Substances
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Peptide Fragments
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Aspartic Acid
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Asparagine
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Phytic Acid
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Oxygen