Molecular dynamics & function of channels


Currently research in my group focuses on theoretical/computational modeling of structure/function relationships and mechanisms of functioning of ion channel and receptor proteins. These proteins are typically constructed as multi-subunit assemblies. Each subunit in turn may consist of several structurally distinct protein domains in a modular fashion. For example, Glutamate Receptors (GluR); are formed as tetramers with a bundle of alpha-helixes spanning the lipid bilayer (biological membrane); and forming a water-filled channel for ion permeation. The channel is gated (opens and closes); when ligand molecules, such as an agonist glutamate, bind to the extracellularly located ligand binding domains of the protein. Passage of a gating signal from the ligand binding to the transmembrane domain is not well understood. We are currently working toward developing theoretical models and computational methodologies which combine hierarchically molecular level description of the protein and its important “chemistry”, e.g. ligand interaction with the ligand binding domain, and a coarse grained description of the protein which will allow us to model interaction and mobility of protein domains and subunits on micro- to millisecond time-scales relevant to the physiological function.



PhD 1998, University of Pittsburgh

Postdoctoral Training

1998-1999, Tel Aviv University, Isreal


Carnegie Mellon University
Department of Chemistry
4400 Fifth ave
Pittsburgh, PA 15213

Phone: (412) 624-8768 


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