Unique Combination of Single Molecule Fluorescence Microscopy and Optical Trapping Reveals Structure & Function of Certain DNA Repair Proteins

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. Scientists who study biological systems at the molecular level have over the years looked to the structure of protein molecules--how the atoms are organized--to shed light on the diverse functions each protein performs in the cell. The inverse is also true: observing the specific work particular protein molecules perform has provided important clues as to the conformation of the respective molecules. But, until recently, our most advanced laboratory experiments could only investigate one at a time--static form or dynamic function--and from the results, deduce the other. This indirect method often doesn't provide definitive answers. Now, Illinois biological physicists Dr. Taekjip Ha and Dr. Yann Chemla have combined two cutting-edge laboratory techniques that, when used together, directly get at the structure-function relationship in proteins. Dr. Ha is well recognized for his innovative single molecule fluorescence microscopy and spectroscopy techniques. Dr. Chemla is a top expert in optical trapping techniques. Their combined method--simultaneous fluorescence microscopy and optical trapping--yields far more definitive answers to questions relating structure to function than either technique could independently. Working in collaboration, Dr. Ha and Dr. Chemla each applied the above techniques in their laboratories, with conclusive results.
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