Abstract
Biological effects of RNA-binding proteins (RBPs) are controlled by the kinetics of RBP association to and dissociation from a given binding site on an RNA. Yet, these kinetics could not be measured in cells. A new method, kinetic crosslinking and immunoprecipitation (KIN-CLIP) now allows the determination of RBP association and dissociation rate constants at thousands of individual binding sites in cells, using a pulsed femtosecond UV laser to efficiently crosslink RNA and proteins.
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