Research
The problems we are currently pursuing explore various aspects of the physics and chemistry of aqueous systems. Our overarching goal is to use theory and simulations to understand how solutes interact with liquid water, the matrix of life.
- Clathrate hydrate formation. Hydrates are crystalline phases of water and dissolved substances, typically natural gas molecules. Clathrates are a promising source of energy, and have also been considered for storing hydrogen gas and for sequestering carbon dioxide. Our goal is to understand the role of hydrate-promoters in the formation and stabilization of the hydrates. Such an understanding can also help us better understand hydrophobic hydration and biological self-assembly.
- Metal-protein interactions. We are developing a statistical mechanical and computational chemistry framework to treat metal-protein interactions. Our long term goal is to understand how metal ions guide the folding of small peptides, a process that may be of relevance to neuro-degenerative diseases such as Alzheimer's and Parkinson's diseases. This effort draws upon our work on understanding the chemistry of ion hydration and ion-protein interactions in ion channels.
- Ion selectivity and regulation of ion channels. Ion channels regulate the voltage across cells and are essential in regulating the behavior of excitable cells, especially nerve cells. Using statistical mechanical theory and molecular dynamics simulations we are exploring how glycosylation alters the voltage sensitivity of the ion channels. Our theory and simulation study is guided by experimental collaborations with researchers at Hopkins, NYU, and Temple.
- Protein solution thermodynamics and phase behavior of proteins. How is it that despite the adventitious interactions within the crowded cellular environment, proteins do not form aggregates and fall out of solution? We are investigating the role of protein hydration in regulating protein-protein interactions. Of particular interest is how mutations in the eye-lens protein gamma-crystallin regulate its solubility.