Thread: NMR paper Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.
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Default Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.
Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.

Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.

J Biomol NMR. 2017 Feb 04;:

Authors: Bauer T, Dotta C, Balacescu L, Gath J, Hunkeler A, Böckmann A, Meier BH

Abstract
The temperature-dependent resonance-line broadening of HET-s(218-289) in its amyloid form is investigated in the range between 110*K and 280*K. Significant differences are observed between residues in the structured hydrophobic triangular core, which are broadened the least and can be detected down to 100*K, and in the solvent-exposed parts, which are broadened the most and often disappear from the observed spectrum around 200*K. Below the freezing of the bulk water, around 273*K, the protein fibrils are still surrounded by a layer of mobile water whose thickness decreases with temperature, leading to drying out of the fibrils.


PMID: 28161758 [PubMed - as supplied by publisher]



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