Yewdall NAAllison TMPearce FGRobinson CVGerrard JA2018-12-052018-12-0520182041-65202041-6539http://hdl.handle.net/10092/16291© The Royal Society of Chemistry. 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.enThis article is licensed under a Creative Commons Attribution 3.0 Unported Licence.Journal Article2018-10-31Field of Research::03 - Chemical Sciences::0303 - Macromolecular and Materials Chemistry::030302 - Nanochemistry and Supramolecular ChemistryFields of Research::31 - Biological sciences::3106 - Industrial biotechnology::310607 - NanobiotechnologyFields of Research::34 - Chemical sciences::3401 - Analytical chemistry::340101 - Analytical spectrometryhttps://doi.org/10.1039/c8sc01379a