Characterization of fibril dynamics on three timescales by solid-state NMR

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 f...

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Bibliographic Details
Published in:Journal of biomolecular NMR 2016-08, Vol.65 (3-4), p.171-191
Main Authors: Smith, Albert A., Testori, Emilie, Cadalbert, Riccardo, Meier, Beat H., Ernst, Matthias
Format: Article
Language:English
Subjects:
Algorithms
Biochemistry
Biological and Medical Physics
Biophysics
Fungal Proteins - chemistry
Isotope Labeling
Magnetic Resonance Spectroscopy - methods
Models, Theoretical
Molecular Structure
Nuclear Magnetic Resonance, Biomolecular - methods
Physics
Physics and Astronomy
Protein Aggregates
Proteins - chemistry
Spectroscopy/Spectrometry
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Description
Summary: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 .
ISSN:0925-2738
1573-5001
DOI:10.1007/s10858-016-0047-8