Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils
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Author / Producer
Date
2017-01
Publication Type
Journal Article
ETH Bibliography
yes
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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.
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Publication status
published
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Journal / series
Volume
67 (1)
Pages / Article No.
51 - 61
Publisher
Springer
Event
Edition / version
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Geographic location
Date collected
Date created
Subject
Fibrils; HET-s; Line broadening; Low-temperature; Protein; Solid-state NMR
Organisational unit
03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
Notes
It was possible to publish this article open access thanks to a Swiss National Licence with the publisher.
Funding
159707 - NMR studies in the Solid State (SNF)
146757 - NMR studies in the Solid State (SNF)
146757 - NMR studies in the Solid State (SNF)