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Twisted Protein Aggregates and Disease: The Stability of Sickle Hemoglobin Fibers

M. S. Turner, R. W. Briehl, F. A. Ferrone, and R. Josephs
Phys. Rev. Lett. 90, 128103 – Published 28 March 2003
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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.

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  • Received 9 October 2002

DOI:https://doi.org/10.1103/PhysRevLett.90.128103

©2003 American Physical Society

Authors & Affiliations

M. S. Turner1,*, R. W. Briehl2, F. A. Ferrone3, and R. Josephs4

  • 1Department of Physics, University of Warwick, Coventry CV4 7AL, United Kingdom
  • 2Departments of Physiology & Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461
  • 3Department of Physics, Drexel University, Philadelphia, Pennsylvania 19104
  • 4Department of Molecular Genetics & Cell Biology, University of Chicago, Chicago, Illinois 60637

  • *Corresponding author.

See Also

All Twisted Up

Lea Winerman
Phys. Rev. Focus 11, 12 (2003)

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Vol. 90, Iss. 12 — 28 March 2003

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