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Self-assembly of toroidal proteins explored using native mass spectrometry† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc01379a
| Content Provider | Semantic Scholar |
|---|---|
| Author | Yewdall, N. Amy Allison, Timothy M. Pearce, Frederick Grant Robinson, Carol V. Gerrard, Juliet A. |
| Copyright Year | 2018 |
| Abstract | The peroxiredoxins are a well characterised family of toroidal proteins which can self-assemble into a striking array of quaternary structures, including protein nanotubes, making them attractive as building blocks for nanotechnology. Tools to characterise these assemblies are currently scarce. Here, assemblies of peroxiredoxin proteins were examined using native mass spectrometry and complementary solution techniques. We demonstrated unequivocally that tube formation is fully reversible, a useful feature in a molecular switch. Simple assembly of individual toroids was shown to be tunable by pH and the presence of a histidine tag. Collision induced dissociation experiments on peroxiredoxin rings revealed a highly unusual symmetrical disassembly pathway, consistent with the structure disassembling as a hexamer of dimers. This study provides the foundation for the rational design and precise characterisation of peroxiredoxin protein structures where self-assembly can be harnessed as a key feature for applications in nanotechnology. |
| Starting Page | 6099 |
| Ending Page | 6106 |
| Page Count | 8 |
| File Format | PDF HTM / HTML |
| DOI | 10.1039/c8sc01379a |
| Alternate Webpage(s) | http://www.rsc.org/suppdata/c8/sc/c8sc01379a/c8sc01379a1.pdf |
| PubMed reference number | 30090298 |
| Alternate Webpage(s) | https://doi.org/10.1039/c8sc01379a |
| Journal | Medline |
| Volume Number | 9 |
| Journal | Chemical science |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
