VÁCHA, Robert and D FRENKEL. Relation between Molecular Shape and the Morphology of Self-Assembling Aggregates: A Simulation Study. Biophysical Journal. Bethesda, USA: Biophysical Society, 2011, vol. 101, No 6, p. 1432-1439. ISSN 0006-3495. doi:10.1016/j.bpj.2011.07.046.
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Basic information
Original name Relation between Molecular Shape and the Morphology of Self-Assembling Aggregates: A Simulation Study
Authors VÁCHA, Robert and D FRENKEL.
Edition Biophysical Journal, Bethesda, USA, Biophysical Society, 2011, 0006-3495.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10610 Biophysics
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 3.653
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1016/j.bpj.2011.07.046
UT WoS 000295197300017
Tags ne MU
Tags International impact, Reviewed
Changed by Changed by: Olga Křížová, učo 56639. Changed: 12. 10. 2012 10:52.
Proteins can aggregate in a wide variety of structures, both compact and extended. We present simulations of a coarse-grained anisotropic model that reproduce many of the experimentally observed aggregate structures. Conversely, all structures predicted by our model have experimental counterparts (ribbons, multistranded fibrils, and vesicles). The model we use is that of a rodlike particle with an attractive (hydrophobic) stripe on its side. Our Monte Carlo simulations show that aggregate morphologies crucially depend on two parameters. The first one is the width of the attractive stripe and the second one is a presence or absence of attractive interactions at the particle ends. These results provide us with a generic insight into the relation between the shape of protein-protein interaction potential and the morphology of protein aggregates.
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