Biological protein pores and pore-forming peptides can generate a pathway for the flux of
ions and other charged or polar molecules across cellular membranes. In nature, these …

A single nanopore represents an amazingly versatile single-molecule probe that can be
employed to reveal several important features of polypeptides, such as their folding state …

Proteins are structurally dynamic macromolecules, and it is challenging to quantify the
conformational properties of their native state in solution. Nanopores can be efficient tools to …

An emerging DNA sequencing technique uses protein or solid-state pores to analyze
individual strands as they are driven in single-file order past a nanoscale sensor,,. However …

Structural complexity of glycans derived from the diversities in composition, linage,
configuration, and branching considerably complicates structural analysis. Nanopore-based …

Both protein and solid-state nanopores are under intense investigation for the analysis of
nucleic acids. A crucial advantage of protein nanopores is that site-directed mutagenesis …

The partitioning of polypeptides into nanoscale transmembrane pores is of fundamental
importance in biology. Examples include protein translocation in the endoplasmic reticulum …

In this paper, we describe resistive-pulse sensing of two large DNAs, a single-stranded
phage DNA (7250 bases) and a double-stranded plasmid DNA (6600 base pairs), using a …

In vitro methods have enabled the rapid and efficient evolution of proteins and successful
generation of novel and highly functional proteins. However, the available methods consider …

Electrophysiological studies of the interaction of polymers with pores formed by bacterial
toxins (1) provide a window on single molecule interaction with proteins in real time,(2) …