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• W2072651465 abstract "Phospholipid headgroups act as major determinants in proper folding of oligomeric membrane proteins. The K+-channel KcsA is the most popular model protein among these complexes. The presence of zwitterionic nonbilayer lipid phosphatidylethanolamine (PE) is crucial for efficient tetramerization and stabilization of KcsA in a lipid bilayer. In this study, the influence of PE on KcsA folding properties was analyzed by tryptophan fluorescence and acrylamide quenching experiments and compared with the effect of anionic phosphatidic acid (PA). The preliminary studies suggest that the small size and hydrogen bonding capability of the PE headgroup influences KcsA folding via a mechanism quite similar to that observed for anionic PA." @default.
• W2072651465 created "2016-06-24" @default.
• W2072651465 creator A5076454686 @default.
• W2072651465 date "2011-07-10" @default.
• W2072651465 modified "2023-10-16" @default.
• W2072651465 title "Do Small Headgroups of Phosphatidylethanolamine and Phosphatidic Acid Lead to a Similar Folding Pattern of the K+ Channel?" @default.
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• W2072651465 doi "https://doi.org/10.1007/s00232-011-9384-4" @default.
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