Structure, thermodynamics, dynamics, and assembly of macromolecules at complex aqueous interfaces

Li, Lijuan
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Garde, Shekhar
Belfort, Georges
Cramer, Steven M.
Keblinski, Pawel
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Chemical engineering
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We extend our research to understand the behavior of water near chemically and topographically complex proteins surfaces. Specifically, we develop a new method based on a gradual drying of the protein hydration shell (using an external potential) to characterize the hydrophobicity of the surface at the nanoscale. Our method is motivated by 'density fluctuations-based' mapping of protein hydrophobicity, but is far more effective and efficient than previous methods. In combination with homology modeling of protein structures and molecular dynamics simulations, we apply the new method to characterize several biological systems -- the protein hydrophobin II and engineered antibodies associated with the Alzheimer's disease. Using the nanoscale characterization of these molecules and their mutants, we obtain insights into their interactions with other molecules and to surfaces. In addition to serving as a practical bridge to fundamental statistical mechanical ideas in the liquid state theory, our method and its applications may help better understand protein-ligand binding, protein aggregation, the rational design of bio-sensing devices and antibody-based drugs.
December 2016
School of Engineering
Dept. of Chemical and Biological Engineering
Rensselaer Polytechnic Institute, Troy, NY
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