A Mass‐Spectrometry‐Based Approach to Distinguish Annular and Specific Lipid Binding to Membrane Proteins

• Published in: Angewandte Chemie International Edition Vol. 59; no. 9; pp. 3523 - 3528
• Main Authors: Bolla, Jani Reddy, Corey, Robin A., Sahin, Cagla, Gault, Joseph, Hummer, Alissa, Hopper, Jonathan T. S., Lane, David P., Drew, David, Allison, Timothy M., Stansfeld, Phillip J., Robinson, Carol V., Landreh, Michael
• Format: Journal Article
• Language: English
• Published: Germany Wiley Subscription Services, Inc 24.02.2020; John Wiley and Sons Inc
• Edition: International ed. in English
• Subjects: Binding; Cardiolipins - chemistry; Cardiolipins - metabolism; Communication; Communications; Detergents; Detergents - chemistry; Dimers; Homology; Leucine; Lipid Bilayers - chemistry; Lipid Bilayers - metabolism; lipid binding; Lipids; Lipids - chemistry; Mass Spectrometry; Mass spectroscopy; membrane protein structure; Membrane proteins; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Membranes; Methanomicrobiaceae - metabolism; Molecular dynamics; Molecular Dynamics Simulation; native mass spectrometry; Presenilin; Presenilins - chemistry; Presenilins - metabolism; Protein Binding; Proteins; Scientific imaging; Spectroscopy; Substrates; native mass spectrometry; membrane protein structure; molecular dynamics; lipid binding

Membrane proteins engage in a variety of contacts with their surrounding lipids, but distinguishing between specifically bound lipids, and non‐specific, annular interactions is a challenging problem. Applying native mass spectrometry to three membrane protein complexes with different lipid‐binding p...