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

J Biomol NMR. 2016 Aug;65(3-4):171-191. doi: 10.1007/s10858-016-0047-8. Epub 2016 Jul 16.

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.

Keywords: Dynamics; Fibrils; Magic-angle spinning; Relaxation; Solid-state NMR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Fungal Proteins / chemistry
  • Isotope Labeling
  • Magnetic Resonance Spectroscopy* / methods
  • Models, Theoretical
  • Molecular Structure
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Protein Aggregates*
  • Proteins / chemistry*

Substances

  • Fungal Proteins
  • HET-S protein, Podospora anserina
  • Protein Aggregates
  • Proteins