biostudies-literatureKumar SWelch FoundationNational Institutes of HealthNIGMS NIH HHS11429-11432https://www.ebi.ac.uk/biostudies/studies/S-EPMC12204147biostudies-literatureUnknown61(61)Membrane protein-lipid interactions, like other biomolecular interactions, are often temperature-sensitive. Here, we use variable-temperature electrospray ionization mass spectrometry to investigate the temperature dependence of protein-lipids interactions from membranes. The findings reveal that specific lipid binding, and in some cases metal ion binding, to membrane proteins is significantly enhanced at elevated temperatures.Chemical communications (Cambridge, England)Temperature-dependence of membrane protein-lipid interactions in membranes.PMC12204147R01GM139876A-2106-20220331R01 GM121751R01 GM139876RM1GM1454316RM1 GM149374RM1GM149374Lantz CLynn MLaganowsky AStover LKumar SDowning JRussell DHfalseTemperature-dependence of membrane protein-lipid interactions in membranes.Membrane protein-lipid interactions, like other biomolecular interactions, are often temperature-sensitive. Here, we use variable-temperature electrospray ionization mass spectrometry to investigate the temperature dependence of protein-lipids interactions from membranes. The findings reveal that specific lipid binding, and in some cases metal ion binding, to membrane proteins is significantly enhanced at elevated temperatures.2025-01-01T00:00:00Z2025 Jul2026-03-27T15:25:31.749Z2025-08-23T03:09:23.466ZS-EPMC122041474057662610.1039/d5cc01576f