Toward Extreme Biophysics: Deciphering the Infrared Response of Biomolecular Solutions at High Pressures. Issue 33 (28th June 2016)

• Record Type: Journal Article
• Authors: Imoto, Sho; Kibies, Patrick; Rosin, Christopher; Winter, Roland; Kast, Stefan M.; Marx, Dominik
• Is Part Of: Angewandte Chemie international edition. Volume 55:Issue 33(2016)
• Page Start: 9534
• Page End: 9538
• Publication Date: 2016-06-28
• Subjects: biophysics -- computational chemistry -- cosolvents -- high-pressure chemistry -- vibrational spectroscopy; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201602757
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: 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. Abstract : 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.