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• W3208650989 abstract "Lipid-protein interactions play an important direct role in the function of many membrane proteins. We argue they are key players in membrane structure, modulate membrane proteins in more subtle ways than direct binding, and are important for understanding the mechanism of classes of hydrophobic drugs. By directly comparing membrane proteins from different families in the same, complex lipid mixture, we found a unique lipid environment for every protein. Extending this work, we identified both differences and similarities in the lipid environment of GPCRs, dependent on which family they belong to and in some cases their conformational state, with particular emphasis on the distribution of cholesterol. More recently, we have been studying modes of coupling between protein conformation and local membrane properties using model proteins. In more applied approaches, we have used similar methods to investigate specific hypotheses on interactions of lipid and lipid-like molecules with ion channels. We conclude this perspective with some considerations for future work, including a new more sophisticated coarse-grained force field (Martini 3), an interactive visual exploration framework, and opportunities to improve sampling." @default.
• W3208650989 created "2021-11-08" @default.
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• W3208650989 date "2021-11-03" @default.
• W3208650989 modified "2023-09-27" @default.
• W3208650989 title "Insights into lipid-protein interactions from computer simulations" @default.
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• W3208650989 doi "https://doi.org/10.1007/s12551-021-00876-9" @default.
• W3208650989 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35047089" @default.
• W3208650989 hasPublicationYear "2021" @default.
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