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• W2910670333 startingPage "1256" @default.
• W2910670333 abstract "It has been extremely challenging to detect protein structures with a dynamic core, such as dry molten globules, that remain in equilibrium with the tightly packed native (N) state and that are important for a myriad of entropy-driven protein functions. Here, we detect the higher entropy conformations of a human serum protein, using red-edge excitation shift experiments. We covalently introduced a fluorophore inside the protein core and observed that in a subset of native population, the side chains of the polar and buried residues have different spatial arrangements than the mean population and that they solvate the fluorophore on a timescale much slower than the nanosecond timescale of fluorescence. Our results provide direct evidence for the dense fluidity of protein core and show that alternate side-chain packing arrangements exist in the core that might be important for multiple binding functions of this protein." @default.
• W2910670333 created "2019-01-25" @default.
• W2910670333 creator A5031633416 @default.
• W2910670333 creator A5080471399 @default.
• W2910670333 date "2019-01-14" @default.
• W2910670333 modified "2023-10-18" @default.
• W2910670333 title "Slow Motion Protein Dance Visualized Using Red-Edge Excitation Shift of a Buried Fluorophore" @default.
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• W2910670333 doi "https://doi.org/10.1021/acs.jpcb.8b11151" @default.
• W2910670333 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30640479" @default.
• W2910670333 hasPublicationYear "2019" @default.
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