The cell membrane is a uniquely complex and dynamic chemical environment. Even a simplistic binary description of an individual lipid molecule as hydrophobic tail and hydrophilic headgroup segments makes for a profoundly intricate environment considering the supramolecular ensemble of many such molecules that make up the membrane bilayer. Added to that are at least two facts that increase the chemical complexity of this environment - i) the cellular lipidome comprises of hundreds of lipid molecules whose spatiotemporal distribution is not static; ii) the membrane bilayer is juxtaposed adjacent to a rich aqueous phase with ions, small molecules and macromolecules ranging from small peptides to large proteins. Clearly, membrane proteins that have evolved to function in this milieu, have very different chemical properties and are governed by radically different constraints than soluble proteins. We as a lab are interested in the structural, chemical and cellular biology of membrane proteins. We are interested in obtaining detailed structural descriptions of membrane proteins and in understanding the connection between their structural chemistry and their biological function and ultimately, how that links to their malfunctioning in human diseases. Towards this end, we are combining high resolution structural techniques such as cryoEM and x-ray crystallography, solution biochemical and biophysical techniques with detergent-solubilized proteins and reconstituted proteoliposomes and in collaboration, high throughput small molecule screening. More recently we have been inspired by our structural and biochemical findings to guide cell biology experiments that we are driving in our lab. We are focusing on two distinct areas - i) membrane-embedded enzymes that catalyze protein lipidation and ii) transporters that move transition metal ions and large organic molecules across the membrane.

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