One of the most effective ways of studying a biological system is to compare the population states of proteins as a function of time and chemical environments. Unfortunately, some of the subpopulations induced by external stimulation are too small and are hidden under ensemble averaging when using traditional methods. In collaboration with Dr. Stephen Quake at Stanford, we have developed a microfluidics based fully automatic single-molecule method capable of resolving subpopulations and monitoring the transition of individual molecules to its various functional states. The microfluidic chip homogenizes a variety of combinations of the source solutions, allowing automated observation under various conditions. On this foundation, we have developed a single-molecule method based on fluorescence resonance energy transfer (FRET) that assays the enzymatic activity of e-coli RNAP by quantifying the amount of mRNA transcripts produced. Using this method we can rapidly screen protein functionality in a large reagent space.

Transcription with a novel high-throughput microfluidic assay

243rd National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.