Data on the target search by a single protein on DNA measured with ultrafast force-clamp spectroscopy

The mechanism by which proteins are able to find small cognate sequences in the range from few to few tens of base pairs amongst the millions of non-specific chromosomal DNA has been puzzling researchers for decades. Single molecule techniques based on fluorescence have been successfully applied to investigate this process but are inherently limited in terms of spatial and temporal resolution. We previously showed that ultrafast force-clamp spectroscopy, a single molecule technique based on laser tweezers, can be applied to the study of protein-DNA interaction attaining sub-millisecond and few base-pair resolution. Here, we share experimental records of interactions between a single lactose repressor protein and DNA collected under different forces using our technique [1]. The data can be valuable for researchers interested in the study of protein-DNA interaction and the mechanism of DNA target search, both from an experimental and modeling point of view. The data is related to the research article "Sliding of a single lac repressor protein along DNA is tuned by DNA sequence and molecular switching" [2].