Biophysical Society 67th Annual Meeting Program Guide

Room 10: Monday, February 20 10:30 AM – 12:00 PM Bruker EPR Research Solutions from Routine Analytics to High-End Experimentation Ralph Weber Bruker EPR presents new hardware and software advances to answer your research needs. NMR Research Solutions for Biophysical Applications Clemens Anklin After the successful introduction of 1.2 GHz magnets, Bruker BioSpin has been able to apply the HTS technology to create a 1.0 GHz system with a significantly smaller footprint. The Ascend EVO 1 GHz magnet operates at 4.2 K, using 1.3 of the amount of helium of previous 1GHz magnets. Due to its reduced height and smaller stray field, it can easily be sited in a single story lab. Other new developments include probes, acquisition, processing, and analysis software. Speakers Clemens Anklin, Vice President of NMR Applications, Bruker BioSpin Corporation Ralph Weber, Senior Applications Scientist, Bruker BioSpin Corporation 12:30 PM – 2:00 PM Leica Microsystems Molecular Interaction Across Imaging Modalities with the Leica STELLARIS Confocal Platform Molecular interactions and dynamics are the foundation of cellular machinery. For molecules to interact, they must come close enough in space so they can exert a chemical influence on their molecular environ ment. Confocal fluorescence imaging became a pillar in such endeavors for the specificity conferred by fluorochromes, and the spatial context, spatial and temporal resolution for the inherent dynamic nature of the interaction process. The ultimate tool of choice to study the interaction of two molecules is Förster Resonant Energy Transfer (FRET), where the molecules of interest are tagged with probes that act as a “donor-acceptor pair” (1). Many FRET approaches rely on intensity-based measurements such as quenching of donor, acceptor photobleaching, and sensitized emission. Intensity-based FRET requires basic instrumentation but has high risks of artifacts from experimental design. The gold standard to measure FRET is FLIM (fluorescence lifetime imag ing microscopy), as the FRET readout here depends only on the donor fluorescence lifetime changes. The analysis of FLIM-FRET can be done by fitting the fluorescence decay with a multi-exponential model or non fitting methods, such as phasor FLIM (2) and minimal fraction of donor molecules (mfD) approach (3). All these approaches are available in the

4:30 PM – 6:00 PM Fluidic Analytics

Introducing Microfluidic Diffusional Sizing (MDS) Technology; Quantify and Characterize any Protein Interaction – Even In Complex Backgrounds, Even with Challenging Targets Studying protein interactions is of fundamental importance in a wide variety of research fields, including neurobiology, oncology, immunol ogy, structural biology, and molecular biology. The more scientists understand about protein interactions, the more we will know about the inner workings of a cell, and crucially, the bet ter we will understand what happens when normal cellular function is subverted in human disease. But, with a multitude of different tech nologies on the market, how do researchers know which technique is right for them? Microfluidic Diffusion Sizing technology (MDS) brings a new tool to the analytical characterization toolbox: a different approach that enables the analysis of protein interactions close to in vivo conditions. Measuring What Matters With MDS, scientists can determine affinity of interaction (KD), concen tration of bound protein, and stoichiometric information, in solution, and all in a single experiment, whether using simple biological buffer systems or complex backgrounds such as serum, plasma, saliva, and cell lysates. The MDS technology enables quantification and characterization of any protein interaction – even in complex backgrounds or with challenging targets • Characterize membrane proteins • Track functional immune response in serum samples • Reveal therapeutic antibody / protein interaction mechanisms • Characterize disordered proteins, higher-order complexes, or amyloids under close to in vivo conditions • Explore aggregation effects and distinguish between specific and non-specific binding During our presentation we will describe a series of case studies and collaborations with pioneering researchers covering such topics: • Purification-free affinity and concentration measurement of membrane-protein targets • Determination of antibody affinities and concentrations directly in clinical samples • In-solution measurement of antibody affinities and binding stoichiometries to neurotoxic amyloid species • Binding of Fc-engineered IgG antibodies to FcRn • In-solution affinity measurement of a drug-induced protein complex Speaker Molly Coseno, Sales Application Specialist, Fluidic Analytics


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