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Updated: Sep 29, 2025
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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
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Tracking local and global structural changes in a protein by cold ion spectroscopy.
Andrei Zviagin1, Vladimir Kopysov1, Natalia S Nagornova1
1Laboratoire de Chimie Physique Moléculaire, École Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland. oleg.boiarkin@epfl.ch.
Physical Chemistry Chemical Physics : PCCP
|March 25, 2022
Summary
Studying native protein structures in the gas phase is difficult. This research uses UV and IR spectroscopy to observe native-like ubiquitin structures, enabled by microhydration and evaporative cooling during ionization.
Area of Science:
- Biophysics
- Structural Biology
- Spectroscopy
Background:
- Characterizing native protein structures in the gas phase is challenging due to conformational changes during desolvation and ionization.
- Understanding these changes is crucial for gas-phase protein studies.
Purpose of the Study:
- To spectroscopically investigate native-like structures of ubiquitin in the gas phase.
- To explore the role of microhydration and ionization conditions in preserving protein structure.
Main Methods:
- Spectroscopic analysis (UV and IR) of cryogenically cooled, protonated ubiquitin and its microhydrated complexes.
- Varying charge states and ionization conditions.
- Utilizing evaporative cooling for microhydrated complexes.
Main Results:
- UV spectra showed distinct changes (redshifted and smooth) for native-like structures compared to unfolded ubiquitin.
- These spectral changes are attributed to specific hydrogen bonding (Tyr hydroxyl to Glu-51 amide).
- IR spectroscopy confirmed global structural changes via redshifts in NH/OH-stretch vibrations.
Conclusions:
- Microhydrated ubiquitin complexes, when evaporatively cooled, can retain native-like conformations in the gas phase.
- Specific hydrogen bonding interactions stabilize these native-like structures.
- This approach enables the study of protein structure in the gas phase under near-native conditions.
