Snapshotting the transient conformations and tracing the multiple pathways of single peptide folding using a solid-state nanopore.

ABSTRACT: A fundamental question relating to protein folding/unfolding is the time evolution of the folding of a protein into its precisely defined native structure. The proper identification of transition conformations is essential for accurately describing the dynamic protein folding/unfolding pathways. Owing to the rapid transitions and sub-nm conformation differences involved, the acquisition of the transient conformations and dynamics of proteins is difficult due to limited instrumental resolution. Using the electrochemical confinement effect of a solid-state nanopore, we were able to snapshot the transient conformations and trace the multiple transition pathways of a single peptide inside a nanopore. By combining the results with a Markov chain model, this new single-molecule technique is appl

SUBMITTER: Liu SC 

PROVIDER: S-EPMC8179386 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature