期刊
CHEMPHYSCHEM
卷 20, 期 2, 页码 311-317出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cphc.201800779
关键词
Amyloids; NMR spectroscopy; prions; protein dynamics; relaxation dispersion
资金
- National Institutes of Health [R01GM094357, R01GM118664, R01GM123743, S10OD012303, P01AI106705, R01NS083687]
- National Science Foundation [MCB-1715174]
- Camille & Henry Dreyfus Foundation (Camille Dreyfus Teacher-Scholar Award)
- European Research Council [ERC-Stg-2012-311318-Prot-Dyn2Function]
Microsecond to millisecond timescale backbone dynamics of the amyloid core residues in Y145Stop human prion protein (PrP) fibrils were investigated by using N-15 rotating frame (R-1 rho) relaxation dispersion solid-state nuclear magnetic resonance spectroscopy over a wide range of spin-lock fields. Numerical simulations enabled the experimental relaxation dispersion profiles for most of the fibril core residues to be modelled by using a two-state exchange process with a common exchange rate of 1000 s(-1), corresponding to protein backbone motion on the timescale of 1 ms, and an excited-state population of 2 %. We also found that the relaxation dispersion profiles for several amino acids positioned near the edges of the most structured regions of the amyloid core were better modelled by assuming somewhat higher excited-state populations (similar to 5-15 %) and faster exchange rate constants, corresponding to protein backbone motions on the timescale of similar to 100-300 mu s. The slow backbone dynamics of the core residues were evaluated in the context of the structural model of human Y145Stop PrP amyloid.
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