Single-molecule imaging of an in vitro-evolved RNA aptamer reveals homogeneous ligand binding kinetics.

ABSTRACT: Many studies of RNA folding and catalysis have revealed conformational heterogeneity, metastable folding intermediates, and long-lived states with distinct catalytic activities. We have developed a single-molecule imaging approach for investigating the functional heterogeneity of in vitro-evolved RNA aptamers. Monitoring the association of fluorescently labeled ligands with individual RNA aptamer molecules has allowed us to record binding events over the course of multiple days, thus providing sufficient statistics to quantitatively define the kinetic properties at the single-molecule level. The ligand binding kinetics of the highly optimized RNA aptamer studied here displays a remarkable degree of uniformity and lack of memory. Such homogeneous behavior is quite different from the heterog

SUBMITTER: Elenko MP 

PROVIDER: S-EPMC2716146 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature