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A kinetic study of ovalbumin fibril formation: the importance of fragmentation and end-joining (CROSBI ID 220161)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Kalapothakis, Jason M.D. ; Morris, Ryan J. ; Szavits-Nossan, Juraj ; Eden, Kym ; Covill, Sam ; Tabor, Sean ; Gillam, Jay ; Barran, Perdita E. ; Allen, Rosalind J. ; MacPhee, Cait E. A kinetic study of ovalbumin fibril formation: the importance of fragmentation and end-joining // Biophysical journal, 108 (2015), 9; 2300-2311. doi: 10.1016/j.bpj.2015.03.021

Podaci o odgovornosti

Kalapothakis, Jason M.D. ; Morris, Ryan J. ; Szavits-Nossan, Juraj ; Eden, Kym ; Covill, Sam ; Tabor, Sean ; Gillam, Jay ; Barran, Perdita E. ; Allen, Rosalind J. ; MacPhee, Cait E.

engleski

A kinetic study of ovalbumin fibril formation: the importance of fragmentation and end-joining

The ability to control the morphologies of biomolecular aggregates is a central objective in the study of self-assembly processes. The development of predictive models offers the surest route for gaining such control. Under the right conditions, proteins will self-assemble into fibers that may rearrange themselves even further to form diverse structures, including the formation of closed loops. In this study, chicken egg white ovalbumin is used as a model for the study of fibril loops. By monitoring the kinetics of self-assembly, we demonstrate that loop formation is a consequence of end-to-end association between protein fibrils. A model of fibril formation kinetics, including end-joining, is developed and solved, showing that end-joining has a distinct effect on the growth of fibrillar mass density (which can be measured experimentally), establishing a link between self-assembly kinetics and the underlying growth mechanism. These results will enable experimentalists to infer fibrillar morphologies from an appropriate analysis of self-assembly kinetic data.

proteins; self-assembly; fibril formation; kinetics; ovalbumin

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Podaci o izdanju

108 (9)

2015.

2300-2311

objavljeno

0006-3495

10.1016/j.bpj.2015.03.021

Povezanost rada

Fizika, Biologija

Poveznice
Indeksiranost