Threading single proteins through pores to compare their energy landscapes.

ABSTRACT: Translocation of proteins is correlated with structural fluctuations that access conformational states higher in free energy than the folded state. We use electric fields at the solid-state nanopore to control the relative free energy and occupancy of different protein conformational states at the single-molecule level. The change in occupancy of different protein conformations as a function of electric field gives rise to shifts in the measured distributions of ionic current blockades and residence times. We probe the statistics of the ionic current blockades and residence times for three mutants of the [Formula: see text]-repressor family in order to determine the number of accessible conformational states of each mutant and evaluate the ruggedness of their free energy landscapes. Transl

SUBMITTER: Tripathi P 

PROVIDER: S-EPMC9522335 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature