In our postgenomic era, understanding of protein–protein interactions by characterizing the structure of the corresponding protein complex is becoming increasingly important. However, many protein complexes are unstable and therefore are difficult to purify.
My new research-line aims at developing a quick and efficient method that is suitable for structural characterization of unstable protein complexes. In this project, single walled carbon nanotubes (SWNTs) are used to ‘fish’ the target protein complex through affinity interaction by chemically binding affinity pairs on SWNT and the target protein complex respectively. A SWNT has a length of up to several micrometers and a diameter of 1-2 nm, so the purification can be handled within a few seconds by straightforward membrane filtration, and the target protein complex exists as single molecule along the SWNT, and will be validated in single particle structure determination by cryo-EM for single particle analysis.