Polymorphism of Sickle Cell Hemoglobin Aggregates: Structural Basis for Limited Radial Growth

Fibers composed of molecules of deoxygenated sickle cell hemoglobin are the basic cause of pathology in sickle cell disease. The hemoglobin molecules in these fibers are arranged in double strands that twist around one another with a long axial repeat. These fibrous aggregates exhibit a pattern of p...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1986-12, Vol.234 (4781), p.1228-1231
Main Authors: Makowski, Lee, Magdoff-Fairchild, Beatrice
Format: Article
Language:English
Subjects:
Actin Cytoskeleton - metabolism
Anemia
Anemia, Sickle Cell - blood
Biological and medical sciences
Blood
Cell aggregates
Crystals
Erythrocytes, Abnormal - metabolism
Fundamental and applied biological sciences. Psychology
Hemoglobin, Sickle - metabolism
Hemoglobinopathies
Hemoglobinopathy
Hemoglobins
Humans
Intermolecular phenomena
Medical research
Miscellaneous
Molecular biology
Molecular biophysics
Molecular interactions
Molecules
Petroleum
Polymorphism, Genetic
Sediments
Sickle cell anemia
Sickles
Sulfides
Terraces
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Summary:Fibers composed of molecules of deoxygenated sickle cell hemoglobin are the basic cause of pathology in sickle cell disease. The hemoglobin molecules in these fibers are arranged in double strands that twist around one another with a long axial repeat. These fibrous aggregates exhibit a pattern of polymorphism in which the ratio of their helical pitch to their radius is approximately constant. The observed ratio agrees with an estimate of its value calculated from the geometric properties of helical assemblies and the degree of distortion that a protein-protein interface can undergo. This agreement indicates that the radius of an aggregate is limited by the maximum possible stretching of double strands. The geometric properties limiting the radial extent of sickle hemoglobin fibers are fundamental to all cables of protein filaments and could contribute to the control of diameter in other biological fibers such as collagen or fibrin.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.3775381