Proline/Alanine Tails as Ionization Enhancement Tags in Native Mass Spectrometry

dc.contributor.authorAbdalla, Marwa
dc.contributor.authorLento, Cristina
dc.contributor.authorJiang, Guifeng
dc.contributor.authorPower, Austin
dc.contributor.authorWilson, Derek
dc.date.accessioned2023-06-08T19:43:17Z
dc.date.available2023-06-08T19:43:17Z
dc.date.issued2023-05-12
dc.description.abstractThis study aimed to study the impact of Proline/Alanine tag on l-asparaginase protein dynamics. Our current analysis demonstrates that the PA tail fragment did not change the core protein dynamics using TRESI HDX MS to provide identical stability with untagged l-asparaginase. Novel Aspects In this work, we propose PASylation ® as a new tool for ionization enhancement through chain ejection.en_US
dc.description.sponsorshipFunding for this work was provided by the Natural Sciences and Engineering Research Council of Canada (NSERC) CRD program. Mitacs program grant collaboration between York University and Jazz Pharmaceuticals. Funded by: funder-id http://dx.doi.org/10.13039/501100000038, Natural Sciences and Engineering Research Council of Canada; Award ID: RGPIN 480432 Funded by: funder-id http://dx.doi.org/10.13039/501100004489, Mitacs;en_US
dc.identifier.citationMarwa ElSabaawy, Cristina Lento and Guifeng Jiang et al. Proline/Alanine Tails as Ionization Enhancement Tags in Native Mass Spectrometry. ScienceOpen Posters. 2023. DOI: 10.14293/P2199-8442.1.SOP-.PYK0FB.v1en_US
dc.identifier.urihttps://doi.org/10.14293/P2199-8442.1.SOP-.PYK0FB.v1en_US
dc.identifier.urihttp://hdl.handle.net/10315/41196
dc.language.isoenen_US
dc.titleProline/Alanine Tails as Ionization Enhancement Tags in Native Mass Spectrometryen_US
dc.typePosteren_US

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