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.identifier.uri |
http://hdl.handle.net/1794/22574 |
|
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.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 |