Related Experiment Video
Updated: Mar 8, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
Published on: September 12, 2019
Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils
Thomas Bauer1, Claudio Dotta1, Livia Balacescu1
1Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, CH-8093, Zurich, Switzerland.
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.
Related Concept Videos
¹H NMR: Interpreting Distorted and Overlapping Signals
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
IR Spectrum Peak Broadening: Hydrogen Bonding
However, the extent of hydrogen bonding influences the observed stretching frequency and band broadening. Intermolecular or intramolecular...
NMR Spectrometers: Resolution and Error Correction
¹³C NMR: ¹H–¹³C Decoupling
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
NMR Spectroscopy: Spin–Spin Coupling

