Nanopore approaches to single-molecule proteomics: From protein sequence to enzyme dynamics

Nanopore currents are emerging as powerful tools for looking at single molecule. Among the advantages of nanopores is that they do not require labeling, and individual molecules can be sampled for up to hours. Nanopore currents can be used for a variety of application, from identifying proteins with single amino acid resolution to monitoring tiny conformational changes in real-time within the entire structure of immobilized proteins. Here I will provide a quick overview on the different approaches our laboratory uses in nanopore proteomics. I will then show examples in which nanopores can be used to monitor conformational dynamics in proteins, suggesting a view of enzyme catalysis in which the soft structure of enzymes guides catalysis through well-defined paths along the reaction coordinates.