Skip to main content
more options

Research Interests

Our research focuses on developing and applying state-of-the-art single-molecule methods to characterize and understand the properties of nanoscale materials and biological systems.  Compared with traditional ensemble measurements, the single molecule approach removes ensemble averaging, so that distributions and fluctuations of molecular properties can be characterized and transient intermediates identified. The single-molecule techqniues we employ include single-molecule fluorescence imaging, single-molecule FRET, single-molecule tracking, super-resolution localization microscopy, and magnetic tweezers. Our research program provides students with scientific training spanning from sophisticated microscopy/spectroscopy techniques, rigorous data analyses to protein and genetic engineering using modern molecular biology techniques, as well as nanotechnology and nanomaterials. Currently our research has the following directions (each with a few exemplary publications).

(1) Single-molecule nanocatalysis.

This research direction in our group is to develop and apply single-molecule methods to study the catalytic, photocatalytic and photoelectrocatalytic properties of nanoscale materials. These materials possess novel or superior catalytic properties compared with their bulk counterparts. Understanding their catalytic properties is important, but hampered by their structural inhomogeneity for ensemble measurements. We are developing novel single-molecule methods to interrogate nanoscale catalysts to understand their structure-function relationships. Currently, we are working on:

(2) Single-molecule bioinorganic chemistry.

Here we develop and apply single-molecule methods to understand how metalloproteins function both in vitro and  living cells. Our current efforts are focused on the protein machineries involved in metal homeostasis in cells:

(3) Protein folding in living cells.

Here we study at the single-molecule level the dynamic processes associated with how a protein is folded once translated from the ribosome inside cells.