The people who burst from bed as the sun rises to cheerily tackle their to-do list—while others sluggishly rouse and fumble with coffee makers—may have a few DNA tweaks in common.
By combining two highly innovative experimental techniques, scientists at the University of Illinois at Urbana-Champaign have for the first time simultaneously observed the structure and the correlated function of specific proteins critical in the repair of DNA, providing definitive answers to some highly debated questions, and opening up new avenues of inquiry and exciting new possibilities for biological engineering.
What was novel wasn’t really the techniques they used, but how they used them. They were able to use high resolution optical traps and single molecule FRET to determine both the processivity of the helicase as well as which conformation the helicase was active in (open or closed) simultaneously. To my knowledge, this hasn’t been done before so that’s pretty cool. They also used this technique to determine that UvrD is far more processive as a dimer than as a monomer.