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• W2945562222 abstract "Significance Protein flexibility is essential for the robustness of biological systems, yet the dynamics underlying this flexibility are difficult to observe, because they are small, fast, and stochastic. Photoprotection in plants is critical for robust growth under highly variable sunlight, but the complexity of photosynthetic proteins means that identifying conformational states and dynamics responsible is challenging. Here, we develop a method using the correlation function of the fluorescence lifetime to characterize multiple dynamical processes in single proteins. By applying this method to the protein Light-Harvesting Complex Stress Related 1 (LHCSR1), we identify two local protein motions that control quenching of excess sunlight, which is a photoprotective effect. Our analytical approach enables a structure-based understanding of the photoprotective mechanisms in green plants." @default.
• W2945562222 created "2019-05-29" @default.
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• W2945562222 date "2019-05-17" @default.
• W2945562222 modified "2023-10-13" @default.
• W2945562222 title "Microsecond and millisecond dynamics in the photosynthetic protein LHCSR1 observed by single-molecule correlation spectroscopy" @default.
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• W2945562222 doi "https://doi.org/10.1073/pnas.1821207116" @default.
• W2945562222 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6561297" @default.
• W2945562222 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31101718" @default.
• W2945562222 hasPublicationYear "2019" @default.
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