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Quantitative FRET (qFRET) Technology for Determination of Protein Interaction Dissociation Constant in the Presence of Other Proteins and Development of Microfluidic Device

  • Author(s): Kung, Raphael Chih-Chung
  • Advisor(s): Liao, Jiayu
  • Grover, William H
  • et al.
Abstract

Post-translational modification is one of the most vital functions at the cellular level in the human body. Ubiquitin and the Ubiquitin-like modifiers (Ubl's) are one class of post-translational modifier. They are involved in a variety of processes including transcription, DNA repair, and tumor progression. Each Ubl alters its target substrates through a 3 step enzymatic cascade of activation by E1, conjugation by E2, and ligation by E3. Our lab has developed a powerful Quantitative FRET analysis method to study the interactions at each step of the post-translational pathway. There are, however, less optimal components of the experimental procedure. The goal of my research is to increase the efficiency of lab protocol by determination of the effect of applying quantitative FRET measurements to unpurified proteins, and explore the possibility of integrating our quantitative FRET technology with microfluidics to enhance the efficiency of lab work.

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