Furthermore, we are interested in proteins which are intrinsically unfolded. Such systems become structured and functional only upon binding a partner, such as another protein or lipid bilayer. Finally, for a number of diseases, such as Alzheimer’s and type II diabetes, the pathology includes proteins that appear to aggregate into a form more stable than their functional precursors.

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Gradinaru biophysics research laboratory at University of Toronto employs advanced laser and detection technology for capturing structural and functional dynamics of individual (bio)molecules. In recent years, single-molecule fluorescence (SMF) has gained considerable ground in life sciences through widespread applications to the study of protein folding and aggregation, enzymatic activity, chemical receptors and biosensors. This popularity is due to a unique capability to "see" details beyond the intrinsic disorder and complexity of biological systems and to better connect with theoretical models. Our group has designed and built several instruments capable of simultaneously measuring multiple characteristics of the weak signals emitted by single fluorescent probes. Remarkably versatile data at the level of single photons is recorded and analyzed by custom software code developed by students in the lab.

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The lab's research focuses on developing nonlinear dynamical techniques and devices to characterize, improve and mimic biological function. His specific interests include: (1) modeling, designing and constructing synthetic gene networks; (2) reverse engineering naturally occurring gene regulatory networks; and (3) developing noise-based sensory prosthetics.

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Our laboratory is interested in the structure and properties of biological membranes. Many cell processes are intimately linked to membranes. These include most signal transduction phenomena, the entry of viruses into target cells, as well as the action of many drugs and cytotoxic agents. We are involved in several studies elucidating the molecular properties of membranes. These include the mechanism of viral fusion and the function of viral fusion proteins; the distribution of cholesterol in membranes and the role of proteinsin sequestering cholesterol-rich domains; the role of lipids in signal transduction; the mechanism of action of antimicrobial peptides and the phenomenon of membrane lysis by different agents leading to cell death. In all of these areas, there is a focus in understanding the relationship between membrane molecular properties and the essential functions of the cell.

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Our group is interested to study structure, dynamics and chemistry in materials confined in various geometries. Materials constrained in one or two dimensions can have different structural or dynamical properties than that of the bulk. In most systems such constraints can change the shape of the potential energy landscape or modify available pathways towards the equilibrium state, thus allowing the formation of structures or chemical and dynamical processes that are not preferable in bulk structures or processes. Examples of such systems of interest are block copolymer self-assemblies in thin film or vesicle geometries, nanocomposite structural and dynamical properties and modified hydrogen bounding structure of water near the solid-liquid and liquid-liquid interfaces. A proper understanding of such differences is important in many technological applications where materials are constrained in nanometer size spaces, such as organic LEDs or electronic circuit fabrication applications and drug delivery methods; or in many biological systems where the exact nature of hydrophobic and hydrophilic interactions are important in understanding the details of chemical reactions.

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We are interested in the underlying mechanism of chromosome and plasmid segregation in bacteria and its evolution. Our recent theoretical studies have shown that polymers in strong confinement, such as chromosomes in bacteria, can partition spontaneously to maximize their conformational entropy. This is a strong indication that, with or without protein-based “mitotic machinery,” conformational entropy provides a primordial driving force of segregation for duplicating bacterial chromosomes. Indeed, the main goal of our research at the Center is to study, both theoretically and experimentally, the role of basic physical principles on the fitness and viability of bacteria in the context of chromosome segregation. For our experimental approach, briefly, we plan to construct an “artificial cell” environment by combining microfluidics and single-molecule manipulation techniques, using which we are hoping to measure the physical forces and dynamics of isolated nucleoids in microchannels.

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The mission of the Laboratory of Membrane Biochemistry & Biophysics (LMBB), established in 1992, is to study the alterations in cell membrane structure and function caused by alcohol abuse with a focus upon polyunsaturated lipids. The lab has a particular emphasis on the most highly unsaturated essential fatty acid found in mammalian tissues, docosahexaenoic acid (DHA). This fatty acid typically occurs as a phospholipid in brain and retinal membranes where it is highly enriched, thus these systems are of great interest to those within the laboratory. A nutritional approach to membrane structure and composition is often taken both with respect to essential fatty acid profiles and alcohol content since these are powerful modulators of lipid content and membrane properties.

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Our group at the Beckman Institute of the University of Illinois utilizes advances in physical theory and computing to model organisms across many levels of organization, from molecules to cells to networks. The research has been driven by problems in biomedicine, such as understanding neural development and processing, solving the mechanisms of bioenergetic proteins like bacteriorhodopsin or light harvesting complexes, the recognition and regulation of DNA by proteins, unraveling the molecular basis of the bodys lipid metabolism and of the mechanical properties of cells, and most recently determining transport through aquaporins.

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