Journal article
Twisted protein aggregates and disease: the stability of sickle hemoglobin fibers
Physical review letters, v 90(12), pp 128103-128103
28 Mar 2003
PMID: 12688906
Featured in Collection : UN Sustainable Development Goals @ Drexel
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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Details
- Title
- Twisted protein aggregates and disease: the stability of sickle hemoglobin fibers
- Creators
- M S Turner - Department of Physics, University of Warwick, Coventry CV4 7AL, United KingdomR W BriehlF A FerroneR Josephs
- Publication Details
- Physical review letters, v 90(12), pp 128103-128103
- Publisher
- Cold Spring Harbor Press; United States
- Grant note
- HL22654 / NHLBI NIH HHS HL 58512 / NHLBI NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:000181862600052
- Scopus ID
- 2-s2.0-84893582884
- Other Identifier
- 991014877956604721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Physics, Multidisciplinary