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• W1988503669 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 heterogeneity seen in previous single-molecule studies of naturally derived RNA and protein enzymes. The single-molecule methods we describe may be of use in analyzing the distribution of functional molecules in heterogeneous evolving populations or even in unselected samples of random sequences." @default.
• W1988503669 created "2016-06-24" @default.
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• W1988503669 date "2009-07-02" @default.
• W1988503669 modified "2023-09-29" @default.
• W1988503669 title "Single-Molecule Imaging of an <i>in Vitro</i>-Evolved RNA Aptamer Reveals Homogeneous Ligand Binding Kinetics" @default.
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• W1988503669 doi "https://doi.org/10.1021/ja901880v" @default.
• W1988503669 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2716146" @default.
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