Sickle Cell Hemoglobin Fiber Structure Altered by α -Chain Mutation

Hybrid hemoglobin molecules prepared with β chains from hemoglobin S (β 6 Glu → Val) and α chains from hemoglobin Sealy (α 47 Asp → 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 ou...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1981-03, Vol.78 (3), p.1406-1410
Main Authors: Crepeau, Richard H., Edelstein, Stuart J., Szalay, Margot, Benesch, Ruth E., Benesch, Reinhold, Kwong, Suzanna, Edalji, Rohinton
Format: Article
Language:English
Subjects:
Biochemistry
Computer simulation
Computers
Density
Electron microscopes
Hemoglobin, Sickle
Hemoglobins
Hemoglobins, Abnormal
Humans
Lead
Macromolecular Substances
Microscopy, Electron
Models, Structural
Molecular structure
Molecules
Mutation
Protein Conformation
Protein Multimerization
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Hybrid hemoglobin molecules prepared with β chains from hemoglobin S (β 6 Glu → Val) and α chains from hemoglobin Sealy (α 47 Asp → 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 α2 Sealyβ2 Shybrid 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:0027-8424
1091-6490
DOI:10.1073/pnas.78.3.1406