The Multiple Roles of Waters in Protein Solvation

Extensive molecular dynamics (MD) simulations have been used to characterize the multiple roles of water in solvating different types of proteins under different environmental conditions. We analyzed a small set of proteins, representative of the most prevalent meta-folds under native conditions, in the presence of crowding agents, and at high temperature with or without high concentration of urea. We considered also a protein in the unfolded state as characterized by NMR and atomistic MD simulations. Our results outline the main characteristics of the hydration environment of proteins and illustrate the dramatic plasticity of water, and its chameleonic ability to stabilize proteins under a variety of conditions.The authors thank INB (Instituto Nacional de Bioinformática) for support in this project. Additional funding to this project comes from H2020 (BioExcel GA 675728, Elixir-Excelerate GA 676559) and the Spanish MINECO (BIO2015/64802-R) funding agencies. IRB Barcelona is recipient of a Severo Ochoa Award of Excellence from MINECO (Government of Spain, GA SEV-2015-050). MO is an ICREA Academia researcher.Peer Reviewe