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• W2895041725 abstract "Membrane protein function fundamentally depends on lipid-bilayer fluidity and the composition of the biological membrane. Although dynamic interdependencies between membrane proteins and the surrounding lipids are suspected, a detailed description is still missing. To uncover lipid-modulated membrane protein backbone dynamics, time-scale-specific NMR relaxation experiments with residue-resolution were recorded. The data revealed that lipid order, modified either biochemically or biophysically, changes the dynamics of the immersed membrane protein in a specific and time-scale-dependent manner. A temperature-dependent dynamics analysis furthermore suggests a direct coupling between lipid and protein dynamics in the picosecond-nanosecond, microsecond, and millisecond time scales, caused by the lipid's trans-gauche isomerization, the segmental and rotational motion of lipids, and the fluidity of the lipid phase, respectively. These observations provide evidence of a direct modulatory capability of the membrane to regulate protein function through lipid dynamics ranging from picoseconds to milliseconds." @default.
• W2895041725 created "2018-10-12" @default.
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• W2895041725 date "2018-10-05" @default.
• W2895041725 modified "2023-10-16" @default.
• W2895041725 title "Lipid- and Cholesterol-Mediated Time-Scale-Specific Modulation of the Outer Membrane Protein X Dynamics in Lipid Bilayers" @default.
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• W2895041725 doi "https://doi.org/10.1021/jacs.8b09188" @default.
• W2895041725 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30289706" @default.
• W2895041725 hasPublicationYear "2018" @default.
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