Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 121, Issue 15, Pages 3636-3643Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.6b09676
Keywords
-
Categories
Funding
- INB (Instituto Nacional de Bioinformatica)
- H2020 (BioExcel) [675728]
- H2020 (Elixir-Excelerate) [676559]
- Spanish MINECO [BIO2015/64802-R]
- Severo Ochoa Award of Excellence from MINECO (Government of Spain) [SEV-2015-050]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available