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• W2004780350 abstract "Hybrid hemoglobin molecules prepared with beta chains from hemoglobin S (beta 6 Glu leads to Val) and alpha chains from hemoglobin Sealy (alpha 47 Asp leads to His) form fibers with a novel structure. In contrast to the typical fibers of hemoglobin S with an average diameter of 22 nm and a solid cross section composed of 10 outer filaments surrounding a 4-filament core, the fibers of the alpha Sealy2 beta S2 hybrid are much larger, with a mean diameter of 32 nm and a unique double-hollow arrangement of filaments. Sealy--S fibers can be described by a model in which the two pairs of filaments most readily lost from fibers of hemoglobin S are missing to form the hollow regions, with an additional sheath of filaments added to form the overall larger structure." @default.
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• W2004780350 date "1981-03-01" @default.
• W2004780350 modified "2023-09-27" @default.
• W2004780350 title "Sickle cell hemoglobin fiber structure altered by alpha-chain mutation." @default.
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• W2004780350 doi "https://doi.org/10.1073/pnas.78.3.1406" @default.
• W2004780350 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/319139" @default.
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