Real-time measurements of dynamic single-molecule interactions: from DNA-binding proteins to molecular motors
May 11 @ 11:00 am - 12:00 pm
Biological processes emerge from mechanisms at the molecular scale. Traditionally, researchers have coupled the use of high-resolution imaging techniques (e.g. X-ray crystallography, cryoEM) with bulk biochemical assays to better understand emergent structure-function relationships. While a useful approach, it does not describe the complete picture when the molecular landscape is diverse and non-Gaussian. Therefore, a method to elucidate both the molecular biophysical and biochemical components is needed to further our understanding of biological processes. Single-molecule force spectroscopy (SMFS) has surfaced as a powerful tool for investigating biophysical properties. When combined with imaging modalities, SMFS tools can enable researchers to examine both biophysical and biochemical properties with unparalleled spatiotemporal insight. Traditionally, these tools were built by labs specializing in SMFS, and their experimental throughput was low. LUMICKS is the first company to combine optical tweezers (the most versatile SMFS tool) with multi-color microscopy to enable simultaneous real-time measurements of sub-picoNetwon forces, sub-nanometer displacements, and diffraction-limited visualization. Our flagship instrument, the C-Trap, enables users to study DNA/RNA-protein interactions, molecular (un)folding dynamics, and molecular motors, to name a few. The C-Trap includes a microfluidic device to vastly increase throughput compared to traditional SMFS techniques, and the workflow can be entirely automated using Python scripts. In the past year, the C-Trap was featured in publications such as Nature, PNAS, and Science. In this talk, optical tweezers will be introduced and their application for studying biological processes will be covered.