NDLI: Sickle cell hemoglobin fiber structure altered by alpha-chain mutation.

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Sickle cell hemoglobin fiber structure altered by alpha-chain mutation.

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Sickle cell hemoglobin fiber structure altered by alpha-chain mutation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Benesch, R. Crepeau, R. H. Kwong, S. Szalay, M. Edelstein, S. J. Edalji, R. Benesch, R. E.
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	78
Language	English
Publisher	National Academy of Sciences
Publisher Date	1981-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hemoglobin, Sickle Mutation Hemoglobins, Abnormal Macromolecular Substances Microscopy, Electron Models, Structural Protein Conformation Protein Multimerization Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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