Characterization of HSP 70 chaperones using a solid-state nanopore Device

The heat shock proteins 70 (HSP70s) are produced by highly conserved genes that play an active role in diverse cellular processes including protein folding, disaggregation, and degradation. Using a solid-state nanopore device, proteins can be detected at a single-molecule level with high sensitivity to their volume, electrical charge, and shape information. This project aims to measure the HSP 70 chaperons using a solid-state nanopore sensing system for voltage dependence and pH dependence. Specifically, we intend to characterize archaeal chaperonin subtypes HSPα (TF56), and HSPβ (TF55) by measuring the ionic current blockages caused by this protein translocation through voltage-biased silicon nitride nanopores in an ionic solution. We plan to estimate the relative charge, shape, and size of protein molecules by the mean amplitude, the time duration, the integral of current blockages, and their distributions. In addition, we plan to further characterize these chaperons using atomic force microscopy and Dynamic light scattering.