Ontology highlight
ABSTRACT:
SUBMITTER: Shim JW
PROVIDER: S-EPMC2657931 | biostudies-literature | 2008 Jul
REPOSITORIES: biostudies-literature
The journal of physical chemistry. B 20080619 28
The alpha-hemolysin (alphaHL) protein pore has many applications in biotechnology. This article describes a single-molecule manipulation system that utilizes the nanocavity enclosed by this pore to noncovalently encapsulate a guest molecule. The guest is the thrombin-binding aptamer (TBA) that folds into the G-quadruplex in the presence of cations. Trapping the G-quadruplex in the nanocavity resulted in characteristic changes to the pore conductance that revealed important molecular processes, i ...[more]