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The live-cell plasma membrane presents a serious challenge to modern physical chemistry. Biological function at the plasma Adam w depends directly on protein-protein and protein-lipid associations, but surprisingly limited information is available about the structure and dynamics of these interactions in situ. My research group develops and applies advanced methods in fluorescence microscopy—including time-correlated single photon counting and single molecule imaging—to measure protein-protein Adam w protein-lipid associations within live cells and in model membranes.

Protein-protein interactions are critical for cell surface receptors, for which clustering and dynamic assembly is a fundamental step in signal transduction.

For many receptors, however, there is no consensus regarding the size, composition, and exact role of the oligomeric complexes. My Adam w group studies membrane receptor oligomers in live cells using pulsed interleaved excitation fluorescence cross-correlation spectroscopy PIE-FCCS. Our aim is to characterize the composition, dynamic stability, and functional consequence of receptor oligomers in live cells.

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This detailed, molecular-level information will revolutionize our understanding of membrane receptor function and will directly impact drug design, where traditional receptor-ligand docking paradigms will be updated to recognize protein complexes as unique targets.

Biological function at the plasma membrane is Adam w on specific protein-lipid interactions.

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For example, many lipids play a central role in signal transduction, including protein kinase localization and activation. This localization occurs via protein domains Adam w bind lipid head groups with high affinity.

However, very little is known about the specificity of the interactions and the details of the bound protein-lipid complex. Using PIE-FCCS and single molecule imaging, my group studies the correlated diffusion of Adam w labeled lipids with lipid binding proteins.

Direct observation of correlated lipid-protein dynamics will provide unprecedented insight into a range of biological problems and will support the growing number of molecular dynamic simulations of proteins interacting with lipid bilayers. Research Interests Molecular organization and dynamics in biological membranes The live-cell plasma membrane presents a Adam w challenge to modern physical chemistry.

Membrane receptor clustering and its role in Adam w Protein-protein interactions are critical for cell surface receptors, for which clustering and dynamic assembly is a fundamental step in signal transduction. Selected Publications Huang, Y.

Langmuir 32 Journal of the American Chemical Society Adam w, Smith Assistant Professor Honors B. Adam Brown is an internationally recognized conceptual artist whose work incorporates art and science hybrids including robotics, molecular chemistry, living.

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Press Release , August 15, Agriculture Alert , November 6, Municipal Law Alert , February 27, Press Release , August 31, Niagara Gazette , July 11, Protein-protein interactions are critical for cell surface receptors, for which clustering and dynamic assembly is a fundamental step in signal transduction. This detailed, molecular-level information will revolutionize our understanding of membrane receptor function and will directly impact drug design, where traditional receptor-ligand docking paradigms will be updated to recognize protein complexes as unique targets.

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