期刊
BIOPHYSICAL JOURNAL
卷 108, 期 9, 页码 2300-2311出版社
CELL PRESS
DOI: 10.1016/j.bpj.2015.03.021
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类别
资金
- Engineering and Physical Sciences Research Council [EP/J007404/1]
- Biotechnology and Biological Sciences Research Council [BB/C00759X/2]
- Royal Society University Research Fellowship
- BBSRC [BB/C00759X/2] Funding Source: UKRI
- EPSRC [EP/J007404/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/C00759X/2] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/J007404/1] Funding Source: researchfish
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.
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