Twisted protein aggregates and disease: the stability of sickle hemoglobin fibers

M. S. Turner, R. W. Briehl, F. A. Ferrone, R. Josephs

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

We describe how twist could play an essential role in stabilizing 20 nm diameter sickle hemoglobin fibers. Our theory successfully reproduces the observed variation of helical pitch length with fiber diameter. With no remaining adjustable parameters it also yields a prediction for the torsional rigidity of sickle hemoglobin fibers that is in good agreement with experiment and hence retains the striking feature that such fibers can be highly mechanically anisotropic, even with a ratio of bending to torsional rigidity of about 50. We discuss how our study might be relevant to the development of treatment strategies.

Original languageEnglish (US)
Pages (from-to)128103
Number of pages1
JournalPhysical Review Letters
Volume90
Issue number12
StatePublished - Mar 28 2003
Externally publishedYes

ASJC Scopus subject areas

  • General Physics and Astronomy

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