Toward Extreme Biophysics: Deciphering the Infrared Response of Biomolecular Solutions at High Pressures

Biophysics under extreme conditions is the fundamental platform for scrutinizing life in unusual habitats, such as those in the deep sea or continental subsurfaces, but also for putative extraterrestrial organisms. Therefore, an important thermodynamic variable to explore is pressure. It is shown th...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2016-08, Vol.55 (33), p.9534-9538
Main Authors: Imoto, Sho, Kibies, Patrick, Rosin, Christopher, Winter, Roland, Kast, Stefan M., Marx, Dominik
Format: Article
Language:English
Subjects:
Biomolecules
Biophysics
Chemical bonds
computational chemistry
cosolvents
Deep sea
Deep sea environments
Denaturation
high-pressure chemistry
Hydrogen bonding
Infrared spectroscopy
Pressure
Proteins
Simulation
Solvation
vibrational spectroscopy
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Summary:Biophysics under extreme conditions is the fundamental platform for scrutinizing life in unusual habitats, such as those in the deep sea or continental subsurfaces, but also for putative extraterrestrial organisms. Therefore, an important thermodynamic variable to explore is pressure. It is shown that the combination of infrared spectroscopy with simulation is an exquisite approach for unraveling the intricate pressure response of the solvation pattern of TMAO in water, which is expected to be transferable to biomolecules in their native solvent. Pressure‐enhanced hydrogen bonding was found for TMAO in water. TMAO is a molecule known to stabilize proteins against pressure‐induced denaturation in deep‐sea organisms. Squeeze it out of them: Trimethylamine N‐oxide (TMAO) is known to stabilize protein structures at extreme pressures, possibly through hydrogen bonding. A combination of FTIR spectroscopy and computer simulation has now been used to connect pressure‐induced changes in the IR spectrum of TMAO (see picture) to a locally enhanced hydrogen‐bonding network at high compression. The insight gained should be transferable to biomolecules in their native solvent.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201602757