UV Fluorescence Polarization as a Means to Investigate Protein Conformational and Mass Change Using Intrinsic Tryptophan Fluorescence in Conjunction with UV-capable Polarizers

The essential amino acid tryptophan is intrinsically fluorescent with excitation in the UV range of the spectrum. This physical characteristic can be used to investigate peptides and proteins that contain this amino acid. This application note describes the use of the Synergy H1 reader in conjunction with UV-capable fluorescence polarizers to investigate conformational and mass changes of proteins in solution.