Double filaments in fibers and crystals of deoxygenated hemoglobin S
Sickle cell hemoglobin (HbS) molecules in solution or in SS erythrocytes (those from individuals homozygous for the sickle hemoglobin gene), when deoxygenated, aggregate to form fibers that pack into paracrystalline arrays. The diminished oxygen affinity of HbS is produced by the polymerization, and the distortion of the pliant erythrocyte membrane is produced by the polymerization, and the distortion of the pliant erythrocyte membrane in sickle cell disease results from the elongation of polymers and their subsequent alignment. One of the important problems to be solved in sickle cell disease is the definition of the intermolecular interactions that stabilize the fiber structure. Knowledge of these interactions might lead to the design of stereospecific antisickling agents for clinical use that could inhibit polymerization or could at least destabilize the fiber.
- Research Organization:
- Columbia Univ., New York, NY (United States)
- OSTI ID:
- 6719221
- Journal Information:
- Biophys. J.; (United States), Vol. 32:1
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ERYTHROCYTES
STRUCTURAL CHEMICAL ANALYSIS
HEMOGLOBIN
AFFINITY
AGGLOMERATION
BIOCHEMICAL REACTION KINETICS
CRYSTAL STRUCTURE
FIBERS
INTERMOLECULAR FORCES
MOLECULAR STRUCTURE
OXYGEN
POLYMERIZATION
SICKLE CELL ANEMIA
VAN DER WAALS FORCES
ANEMIAS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
DISEASES
ELEMENTS
GLOBIN
HEMIC DISEASES
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
KINETICS
MATERIALS
NONMETALS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PIGMENTS
PORPHYRINS
PROTEINS
REACTION KINETICS
SYMPTOMS
550200* - Biochemistry
551000 - Physiological Systems