Albany 2015:Book of Abstracts
June 9-13 2015
©Adenine Press (2012)
Water near Proteins and Interfaces: A New Molecular Perspective
Water molecules organize themselves differently near hydrophobic, hydrophilic, and ionic solutes, and near interfaces that include a combination of these characteristics. Such structural organization of water leads to water-mediated interactions (e.g., hydrophobic or ion-ion interactions), which play an important role in many self-assembly processes in aqueous solution. Naturally, characterizing and quantifying hydrophobicity of complex heterogeneous surfaces is important, but has remained a significant challenge. I will present a new molecular level perspective based on theory and atomistic simulations that highlights the role of nanoscale water density fluctuations as a robust signature of hydrophobicity or philicity of complex interfaces. We are developing new computational tools based on this idea to incorporate molecular level information about water into predictive approaches for protein-ligand interactions. Finally, I will present examples demonstrating that distinct behavior of water near extended hydrophobic interfaces - such as the air-water interface - influences water-mediated interactions between hydrophobic solutes or between ions, self-assembly, and aggregation phenomena at interfaces in unique and unexpected ways.
This research is supported by the National Science Foundation. References
V. Venkateshwaran, S. Vembanur, and S. Garde, On the enhancement of water-mediated ion-ion interactions at the water vapor-liquid interface, Proc. Natl. Acad. Sci. USA, 111 (24), 8729-8734 (2014).
A. J. Patel and S. Garde, An Efficient Method to Characterize the Context-Dependent Hydrophobicity of Proteins, J. Phys. Chem. B, 118 (6), 1564-1573 (2014). Featured on the Cover.
Department of Chemical and Biological Engineering