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Proceedings Paper

Intermolecular contacts within sickle hemoglobin fibers
Author(s): Stanley J. Watowich; Leon J. Gross; Robert Josephs
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Paper Abstract

We have combined x-ray crystallographic coordinates of sickle hemoglobin (HbS) molecules with electron microscopic 3-D reconstruction data of HbS fibers to calculate residues involved in intermolecular contacts within the clinically relevant HbS fiber. The model accounts for the action of 80 of the fifty five point mutations of HbS whose effect on fiber formation has been studied. For instance fiber formation is affected by thirty-three mutants. Of these mutants thirty-one occur at the calculated intermolecular contact sites. Fiber formation is not affected by 28 known HbS mutants 16 of these mutations occur at residues not involved in intermolecular contacts. The 12 mutations that occur at contact sites are postulated to not significantly increase fiber formation energy. The number of intermolecular contacts decreases with radius until at the periphery of the particle there are no contacts. We suggest that this observation accounts for the limited radial growth of the particle and that a similar mechanism may be a factor in limiting the size of other helical particles.

Paper Details

Date Published: 1 March 1991
PDF: 8 pages
Proc. SPIE 1396, Applications of Optical Engineering: Proceedings of OE/Midwest '90, (1 March 1991); doi: 10.1117/12.25825
Show Author Affiliations
Stanley J. Watowich, Univ. of Chicago (United States)
Leon J. Gross, Univ. of Chicago (United States)
Robert Josephs, Univ. of Chicago (United States)


Published in SPIE Proceedings Vol. 1396:
Applications of Optical Engineering: Proceedings of OE/Midwest '90

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