Nature has developed corresponding mechanisms to deal with different adverse environmental conditions. For example, when experiencing hyperosmolality, cells will use various small organic molecules as osmolytes to cope with the underlying osmotic stress. However, depending on its chemical structure, an osmolyte can engage in direct and/or indirect interactions with biological molecules, affecting their stability and/or activity. Because these interactions take place in a complex environment, assessing their molecular details is a challenging task. In this talk, we will discuss our recent efforts to tackle this challenge. In particular, we will describe how unnatural amino acids that have unique spectroscopic properties can be used to provide microscopic and site-specific information about the protein-osmolyte interactions in question. Specific examples will be given to highlight how results obtained from such studies can help better understand the mechanism of action of several commonly encountered osmolytes, including urea and its methyl derivatives, glycine betaine (GB), and trimethylamine N-oxide (TMAO).<br/>

Site-specific assessment of biomolecular interactions in osmolyte solutions

ACS Fall 2020 Virtual Meeting

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