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Journal article
A model for the sickle hemoglobin fiber using both mutation sites
Protein science, v 9(5), pp 1031-1034
May 2000
PMID: 10850813
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The standard molecular model of the fiber of the
sickle hemoglobin (HbS: β6 Glu → Val) has been
revised to allow both β6 mutation sites to participate
in intermolecular contacts, rather than only one β6
site as previously thought, for four molecules per 14-molecule
fiber cross section. This structure accurately predicts
the copolymerization of hybridized mixtures of HbS with
HbA or HbC (β6 Glu → Lys), which could not be
reconciled with prior models in which only half the β6
sites were required for assembly. This model suggests new
contacts within the fiber and raises the question of whether
these cross-linked double strands could possess added stability
important in such processes as nucleation.
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Details
- Title
- A model for the sickle hemoglobin fiber using both mutation sites
- Creators
- ADAM Roufberg - Drexel UniversityFRANK A. Ferrone - Drexel University
- Publication Details
- Protein science, v 9(5), pp 1031-1034
- Publisher
- Cambridge University Press
- Number of pages
- 4
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:000087245400021
- Scopus ID
- 2-s2.0-0034119453
- Other Identifier
- 991019168686104721
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- Web of Science research areas
- Biochemistry & Molecular Biology