Megan A. Ewbank

Apr 1, 2024 | pubs.acs.org | Hiruni S. Jayasekera |Farhana Afrin Mohona |Megan A. Ewbank |Michael Marty

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Apr 1, 2024 | dx.doi.org | Hiruni S. Jayasekera |Farhana Afrin Mohona |Megan A. Ewbank |Michael Marty

Download Hi-Res ImageDownload to MS-PowerPointCite This:Anal. Chem. 2024, XXXX, XXX Terms & Conditions Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses).

Sep 22, 2023 | biorxiv.org | Megan A. Ewbank |Michael Marty |Hiruni S. Jayasekera |Farhana Afrin Mohona

AbstractLipids are critical modulators of membrane protein structure and function. However, it is challenging to investigate the thermodynamics of protein-lipid interactions because lipids can simultaneously bind membrane proteins at different sites with different specificities. Here, we developed a native mass spectrometry (MS) approach using single and double mutants to measure the relative energetic contributions of specific residues on Aquaporin Z (AqpZ) toward cardiolipin (CL) binding.