Protein Fluorescence Spectroscopy: PFAST Project www.pfast.phys.uri.edu

Fluorescence spectroscopy is one of the traditional and widely used methods for the investigation of protein structure, conformations, and dynamics. One of the major goals in appling tryptophan fluorescence spectroscopy is to interpret the fluorescence properties in terms of structural parameters and to predict the structural changes in protein. The biggest issue in analyzing spectral data is the complex nature of tryptophan fluorescence, since the majority of proteins contain more than one tryptophan residue. We have designed mathematical methods of spectral analysis (which allow the decomposition of complex spectrum into spectra of individual tryptophan residues), created computational approaches of protein structural analysis and applied the multivariate statistical approaches to establish the correlation between protein spectral and structural properties. Recently we created the first database of combined protein spectral and structural properties. PFAST – Protein Fluorescence And Structural Toolkit: www.pfast.phys.uri.edu is a web-based toolkit. PFAST contains a database of protein fluorescence and structural properties as well as programs for their analysis. Particularly, it allows the user to: 1) analyze fluorescence data (decomposition algorithms); 2) compute structural properties (algorithms for the calculation of structural parameters of the tryptophan environment from atomic structures of proteins from PDB); 3) classify the fluorescence and structural properties and assign the tryptophan residues to spectral and structural classes.

alt PFAST 

Assignment of the spectral component to the tryptophan residues in proteins