Single-molecule spectroscopy is a powerful methodology to characterize inhomogeneous samples 1-4 because information may be hidden or lost in conventional ensemble-averaged experiments due to intrinsic sample heterogeneities 5-7. Here we report a single-molecule spectroscopy study that reveals dynamics of fluctuating molecular noncovalent interactions within single protein-DNA complexes. This data will facilitate a molecule-level understanding for the dynamic mechanisms of the damage-recognition process in DNA repair 8.
Revised: January 12, 2012 |
Published: August 22, 2001
Citation
Lu H.P., L.M. Lakoucheva, and E.J. Ackerman. 2001.Single-Molecule Conformational Dynamics of Fluctuating Noncovalent DNA-Protein Interactions in DNA Damage Recognition.Journal of the American Chemical Society 123, no. 37:9184-9185.PNNL-SA-35320.