Rising, Anna
- Department of Animal Biosciences, Swedish University of Agricultural Sciences
- Karolinska Institute
Abstract
Despite their fundamental biological importance and therapeutic potential, the interactions between chemical chaperones and proteins remain difficult to capture due to their transient and nonspecific nature. Using a simple mass spectrometric assay, we are able to follow the interactions between proteins and the chemical chaperone trimethylamine-N-oxide (TMAO). In this manner, we directly observe that the counteraction of TMAO and the denaturant urea is driven by the exclusion of TMAO from the protein surface, whereas the surfactant lauryl dimethylamine-N-oxide cannot be displaced. Our results clearly demonstrate a direct chaperoning mechanism for TMAO, corroborating extensive computational studies, and pave the way for the use of nondenaturing mass spectrometry and related techniques to study chemical chaperones in molecular detail.
Published in
Journal of Physical Chemistry Letters
2018, volume: 9, number: 14, pages: 4082-4086
Publisher: AMER CHEMICAL SOC
SLU Authors
UKÄ Subject classification
Microbiology
Publication identifier
- DOI: https://doi.org/10.1021/acs.jpclett.8b01817
Permanent link to this page (URI)
https://res.slu.se/id/publ/97019