without changing your settings we'll assume you are happy to receive all RSC cookies.
You can change your cookie settings by navigating to our Privacy and Cookies page and following the instructions. These instructions
are also obtainable from the privacy link at the bottom of any RSC page.
Numerous cellular cosolutes significantly impact the way that proteins and other biomacromolecules act and interact. We have followed the thermodynamic effect of several cosolute classes, including polymers, cellular osmolytes, and inorganic salts, on the stability of biomolecular folding and complexation. By comparing changes in free energy, enthalpy, and entropy upon cosolutes addition for these processes, we identify several thermodynamically distinct mechanisms. Surprisingly, even while many cosolutes display similar scaling of the change in stabilizing free energy with their concentration, a breakdown of this free energy into enthalpic and entropic contributions distinguishes different families of cosolutes. We discuss how these “thermodynamic fingerprints” can direct towards possible underlying mechanisms that govern the cosolute effect.
Fetching data from CrossRef. This may take some time to load.