Investigation of Pore-Forming Transmembrane Toxins using Native Ion-Mobility Mass Spectrometry
| dc.contributor.author | Young, Isabella | |
| dc.date.accessioned | 2017-08-14T17:19:13Z | |
| dc.date.available | 2017-08-14T17:19:13Z | |
| dc.date.issued | 2017 | |
| dc.description | 1 page poster | en_US |
| dc.description.abstract | Antrhax toxin (ATX) and Alpha-Hemolysin (AHL) are examples of large transmembrane pore-forming toxins that are similar in structure and are proposed to have specific protein-lipin interactions. Due to the difficulty of studying these structures in solution, native mass spectrometry (native-MS) was used to examine the structure, stoichiometry, and lipid-binding of these membrane protein complexes and ion mobility (IM) analysis was used to further study the complexes' shape and size. | en_US |
| dc.description.sponsorship | This material is based upon work supported by the National Science Foundation award #1460735. | en_US |
| dc.identifier.uri | https://hdl.handle.net/1794/22574 | |
| dc.language.iso | en | en_US |
| dc.rights | Creative Commons BY-NC-ND 4.0-US | en_US |
| dc.title | Investigation of Pore-Forming Transmembrane Toxins using Native Ion-Mobility Mass Spectrometry | en_US |
| dc.type | Other | en_US |