Abstract
We are using single-pair Förster resonance energy transfer (spFRET) to characterize the conformational kinetics of single Holliday junctions (HJs). By comparing such kinetics in the absence and presence of various HJ-binding proteins we aim to gain some understanding of how HJ structures are recognized and processed in vivo as well as how processes such as HJ branch migration are regulated. Addtionally, we plan to use our system to make quantitative measurements of protein binding energies.
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