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A collaboration between the Photophysics Group at Strathclyde University and Glasgow based HORIBA Jobin Yvon IBH Ltd has created new opportunities for researching proteins and immunoassays. In a breakthrough to be reported in Measurement Science and Technology the Glasgow team describe the excitation of protein fluorescence decay for the first time using a light emitting diode (LED). Hitherto, the shortest wavelength for exciting fluorescence with pulsed sources was 370 nm, but the Glasgow team have demonstrated a new limit of 280 nm by exciting the intrinsic protein fluorescence of the amino acids tryptophan and tyrosine using 600 ps LED pulses at 1 MHz.

Professor David Birch, Head of the Department of Physics at Strathclyde University, explained how proteins are fundamental to life and how a better understanding of the mechanisms by which each protein folds to a unique conformation could aid disease detection and treatment. Time-resolved fluorescence is one of the techniques assisting this goal as it can track molecular dynamics, but until recently fluorescence decay research required a spark source, expensive laser system or synchrotron. Birch went on to explain how a low cost and reliable source for exciting proteins had been long-waited and that the 280 nm pulsed LED will impact even wider across the disciplines. A paper "A new sub-nanosecond LED at 280 nm: application to protein fluorescence" can be found at http://stacks.iop.org/MST/15/L19