Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.
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.
Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093, Zurich, Switzerland.
Thomas
T
Bauer
Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093, Zurich, Switzerland.
Claudio
C
Dotta
Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093, Zurich, Switzerland.
Livia
L
Balacescu
Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093, Zurich, Switzerland.
Julia
J
Gath
Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093, Zurich, Switzerland.
Andreas
A
Hunkeler
Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS, Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France. a.bockmann@ibcp.fr.
Anja
A
Böckmann
Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093, Zurich, Switzerland. beme@ethz.ch.
Beat H
0000-0002-9107-4464
BH
Meier
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D011487:Protein Conformation; D013696:Temperature
D000682:Amyloid
Fibrils; HET-s; Line broadening; Low-temperature; Protein; Solid-state NMR