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• W2588136201 abstract "We compared the dynamics of key methionine methyl groups in the water-accessible hydrophobic cavity of amyloid fibrils and Fluorenylmethyloxycarbonyl-Methionine (FMOC-Met), which renders general hydrophobicity to the environment without the complexity of the protein. Met35 in the hydrated cavity was recently found to undergo a dynamical cross-over from the dominance of methyl rotations at low temperatures to the dominance of diffusive motion of methyl axis at high temperatures. Current results indicate that in FMOC-Met this cross-over is suppressed, similar to what was observed for the dry fibrils, indicating that hydration of the cavity is driving the onset of the dynamical transition." @default.
• W2588136201 created "2017-02-24" @default.
• W2588136201 creator A5011094893 @default.
• W2588136201 creator A5088220999 @default.
• W2588136201 date "2017-04-01" @default.
• W2588136201 modified "2023-09-25" @default.
• W2588136201 title "Comparative dynamics of methionine side-chain in FMOC-methionine and in amyloid fibrils" @default.
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• W2588136201 doi "https://doi.org/10.1016/j.cplett.2017.02.021" @default.
• W2588136201 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5612497" @default.
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