Intermolecular contacts within sickle hemoglobin fibers

Stanley J. Watowich, Leon J. Gross, Robert Josephs

Research output: Contribution to journalLetterpeer-review

44 Scopus citations


By combining X-ray crystallographic co-ordinates of sickle hemoglobin (HbS) molecules with three-dimensional reconstructions of electron micrographs of HbS fibers we have synthesized a model for the structure of the clinically relevant HbS fiber. This model largely accounts for the action of 55 point mutations of HbS whose effect on fiber formation has been studied. In addition, it predicts locations at which additional point mutations are likely to affect fiber formation. The number of intermolecular axial contacts decreases with radius until, at the periphery of the fiber, there are essentially no axial contacts. We suggest that this observation accounts for the limited radial growth of the HbS fiber and that a similar mechanism may be a factor in limiting the size of other helical particles. The methodology for the synthesis of the fiber model is applicable to other systems in which X-ray crystallographic and electron microscopic data are available.

Original languageEnglish (US)
Pages (from-to)821-828
Number of pages8
JournalJournal of Molecular Biology
Issue number4
StatePublished - Oct 20 1989
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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