ResourceSpectroscopy

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

13 Oct 2014

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.

Agilent BioTek Synergy H1 Multimode Reader

Agilent Technologies

Agilent BioTek Synergy H1 is a modular multi-mode microplate reader, with monochromator-based optics and filter-based optics. The proprietary Hybrid Technology offers flexibility and sensitivity across a broad range of applications. The modular platform allows upgrading to expand functionality as your laboratory workflows change.

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