Researchers describe the role of water in protein folding

Giancarlo Franzese, professor in the Department of Fundamental Physics of the UB and leader of the study, explains that "so far, data came from experiments and theories based on hypotheses that are hard to prove and simulations that work only under conditions of high pressure and temperature, but they failed under conditions of low pressure and temperature."

Knowledge about how water works at the protein interface has enabled the research team to prove that "increased stability of hydrogen bonds at molecular hydrophobic interfaces and increased compressibility at these interfaces allow understanding how water contributes to protein folding in a wide range of pressures and temperatures," explains Valentino Bianco that developed this work as part of his doctoral thesis.

It is important to highlight that protein folding is not only due to water activity as protein waste interactions and the presence of cavities also play an important role in the process. The importance of the study relies on the fact that, by using Monte Carlo simulations, it proves that the water unique properties are key to understand protein folding mechanisms and biological function. "The study highlights that water is essential for life, and it can be useful to develop advanced computational tools for protein engineering that can be used in medicine," concluded Franzese.