Anomalous Dynamics of Water Confined in Protein–Protein and Protein–DNA Interfaces
- 26 September 2016
- journal article
- research article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry Letters
- Vol. 7 (19), 3967-3972
- https://doi.org/10.1021/acs.jpclett.6b01858
Abstract
Confined water often exhibits anomalous properties not observable in the bulk phase. Although water in hydrophobic confinement has been the focus of intense investigation, the behavior of water confined between hydrophilic surfaces, which are more frequently found in biological systems, has not been fully explored. Here, we investigate using molecular dynamics simulations dynamical properties of the water confined in hydrophilic protein–protein and protein–DNA interfaces. We find that the interfacial water exhibits glassy slow relaxations even at 300 K. In particular, the rotational dynamics show a logarithmic decay that was observed in glass-forming liquids at deeply supercooled states. We argue that such slow water dynamics are indeed induced by the hydrophilic binding surfaces, which is in opposition to the picture that the hydration water slaves protein motions. Our results will significantly impact the view on the role of water in biomolecular interactions.Funding Information
- Samsung Science and Technology Foundation (SSTF-BA1401-13)
This publication has 37 references indexed in Scilit:
- Water in Nonpolar Confinement: From Nanotubes to Proteins and BeyondAnnual Review of Physical Chemistry, 2008
- Water as an Active Constituent in Cell BiologyChemical Reviews, 2007
- Do we underestimate the importance of water in cell biology?Nature Reviews Molecular Cell Biology, 2006
- WATER MEDIATION IN PROTEIN FOLDING AND MOLECULAR RECOGNITIONAnnual Review of Biophysics and Biophysical Chemistry, 2006
- Interfaces and the driving force of hydrophobic assemblyNature, 2005
- Statistical analysis of predominantly transient protein-protein interfacesProteins-Structure Function and Bioinformatics, 2005
- Role of Water Mediated Interactions in Protein−Protein Recognition LandscapesJournal of the American Chemical Society, 2003
- Dominant forces in protein foldingBiochemistry, 1990
- The Hydrophobic Effect and the Organization of Living MatterScience, 1978
- Some Factors in the Interpretation of Protein DenaturationAdvances in protein chemistry, 1959