We primarily use AFM-based single molecule force spectroscopy (SMFS) and molecular dynamics simulations to examine the mechanical and folding behavior of wild type ankyrin repeat proteins and their mutants.
We use AFM imaging, AFM pulling, in vivo and in vitro protein expression to examine the folding of proteins at the single-molecule level.
We use AFM and computational approaches to investigate the elasticity of single-stranded DNA and force-induced conformational transitions in ssDNA.
We adapt and develop various single-molecule approaches to study the interaction of MMR proteins among themselves and with heteroduplex DNA to elucidate the mechanism of MMR initiation.
We have been working to make it easier for unbiased selection of data and have developed some software which can be accessed here.