Electron transfer challenges common fluorescence technique
Monday, April 20, 2015 - 14:10
in Physics & Chemistry
Tryptophan is an amino acid, one of the building blocks of proteins. It is used extensively to study how proteins change their 3D structure, and also how they interact with other proteins and molecules. This is studied with a fluorescence technique called FRET, which measures the transfer of energy from tryptophan to another molecule. But in some cases, FRET data could be distorted because tryptophan transfers an electron instead of energy. Using a unique spectroscopic technique, scientists at EPFL have now confirmed for the first time that this is indeed the case. The study, which has far-reaching implications for the effectiveness of FRET, is published in PNAS.