Transimpedance Amplifier for Polymer Photodiodes

Dr. Braun’s students in the Polymer Electronics Lab currently have a way to measure the light intensity from their light emitting devices however it consumes an unnecessary amount of space and power. I offer to improve upon the existing transimpedance circuit that Dr. Braun currently uses, reducing the total space occupied by the circuit and the power consumption of the current setup. The transimpedance circuit measures the incidence light intensity from the polymer-based photo detector and outputs an accurate, discrete, and measurable voltage. The current setup however utilizes two 20V wall warts for the positive and negative rails of the transimpedance amplifier. I plan to reduce the two 20V wall warts to a single 12V wall wart. Because of this, difficulty arises from both producing accurate voltage values near the negative rail, or ground, using a single supply, and from measuring the light intensity accurately without additional readings from noise and bias offsets. The current produced from the photo-sensor ranges from pico- to micro- amps, which is a sensitive domain to noise

Virtual Target Screening: Validation Using Kinase Inhibitors

Computational methods involving virtual screening could potentially be employed to discover new biomolecular targets for an individual molecule of interest (MOI). However, existing scoring functions may not accurately differentiate proteins to which the MOI binds from a larger set of macromolecules in a protein structural database. An MOI will most likely have varying degrees of predicted binding affinities to many protein targets. However, correctly interpreting a docking score as a hit for the MOI docked to any individual protein can be problematic. In our method, which we term “Virtual Target Screening (VTS)”, a set of small drug-like molecules are docked against each structure in the protein library to produce benchmark statistics. This calibration provides a reference for each protein so that hits can be identified for an MOI. VTS can then be used as tool for: drug repositioning (repurposing), specificity and toxicity testing, identifying potential metabolites, probing protein structures for allosteric sites, and testing focused libraries (collection of MOIs with similar chemotypes) for selectivity. To validate our VTS method, twenty kinase inhibitors were docked to a collection of calibrated protein structures. Here we report our results where VTS predicted protein kinases as hits in preference to other proteins in our database. Concurrently, a graphical interface for VTS was developed