Sickle cell hemoglobin fiber structure altered by alpha-chain mutation.
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.
D003201:Computers; D006451:Hemoglobin, Sickle; D006455:Hemoglobins, Abnormal; D006801:Humans; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008961:Models, Structural; D009154:Mutation; D011487:Protein Conformation; D055503:Protein Multimerization
D006451:Hemoglobin, Sickle; D006455:Hemoglobins, Abnormal; D046911:Macromolecular Substances; C029985:hemoglobin Sealy