Collaboration sheds new light on proteins
A collaboration between the Photophysics Group at Strathclyde University and Glasgow-based HORIBA Jobin Yvon IBH has created new opportunities for researching proteins and immunoassays.
A collaboration between the Photophysics Group at Strathclyde University and Glasgow-based HORIBA Jobin Yvon IBH has created new opportunities for researching proteins and immunoassays.
Hitherto, the shortest wavelength for exciting protein fluorescence decay with pulsed sources was 370nm, but the Glasgow team has demonstrated a new limit of 280nm by exciting the intrinsic protein fluorescence of the amino acids tryptophan and tyrosine using 600ps LED pulses at 1 MHz.
Time-resolved fluorescence is one of the techniques assisting the understanding of the mechanisms by which each protein folds to a unique conformation, which in turn aid disease detection and treatment, explained Professor David Birch, head of the department of physics at Strathclyde University.
Until recently fluorescence decay research re-quired a spark source, expensive laser system or synchrotron. However, Birch said a low cost and reliable source for exciting proteins had been long-waited and that the 280nm pulsed LED will impact even wider across the disciplines.