title: Characterization of fibril dynamics on three timescales by solid-state NMR.
abstract: A multi-timescale analysis of the backbone dynamics of HET-s (218-289) fibrils is described based on multiple site-specific R 1 and R 1ρ data sets and S (2) measurements via REDOR for most backbone (15)N and (13)Cα nuclei. (15)N and (13)Cα data are fitted with motions at three timescales. Slow motion is found, indicating a global fibril motion. We further investigate the effect of (13)C-(13)C transfer in measurement of (13)Cα R 1. Finally, we show that it is necessary to go beyond the Redfield approximation for slow motions in order to obtain accurate numerical values for R 1ρ.
authors.affiliation: Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland.
authors.forename: Albert A
authors.initials: AA
authors.lastname: Smith
authors.affiliation: Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland.
authors.forename: Emilie
authors.initials: E
authors.lastname: Testori
authors.affiliation: Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland.
authors.forename: Riccardo
authors.initials: R
authors.lastname: Cadalbert
authors.affiliation: Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland. beme@ethz.ch.
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
authors.affiliation: Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland. maer@ethz.ch.
authors.forename: Matthias
authors.initials: M
authors.lastname: Ernst
mesh_terms: D000465:Algorithms; D005656:Fungal Proteins / Q000737:chemistry; D007553:Isotope Labeling; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008962:Models, Theoretical; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D066329:Protein Aggregates; D011506:Proteins / Q000737:chemistry*
chemical_list: D005656:Fungal Proteins; C083891:HET-S protein, Podospora anserina; D066329:Protein Aggregates; D011506:Proteins
keywords: Dynamics; Fibrils; Magic-angle spinning; Relaxation; Solid-state NMR