Fluorescence Spectroscopy of Intrinsically Disordered Proteins

Abstract

11Fluorescence spectroscopy can be successfully used in studies of intrinsically disordered proteins (IDPs). IDPs are usually characterized by surface location of tryptophan residues with redshifted tryptophan fl uorescence spectra with maxima at 340 -353 nm. Such tryptophans are readily accessible to external fl uorescence quenchers. Interactions of these proteins with another proteins and peptides usually transfer tryptophan residues to a more hydrophobic or more rigid environment, which results in a blueshift of fl uorescence maximum position. These spectral effects can be used for evaluation of interaction parameters. Spectral probes and labels are also widely used for the investigation of natively disordered proteins. ANS and bis -ANS have a tendency to bind to IDPs, but not to the tightly packed ordered proteins. ABSTRACT

Analyzing the structural and functional roles of residues from the ‘black’ and ‘gray’ clusters of human S100P protein

“…for review see [50]). Table 2S shows fluorescence parameters of bis-ANS bound to S100P and its cluster mutants under variety of conditions.…”

Comprehensive analysis of the roles of ‘black’ and ‘gray’ clusters in structure and function of rat β-parvalbumin

“…Structural compactness of rat β-PA and its cluster mutants was studied by means of fluorescent probe bis-ANS. A transition of bis-ANS (and 8-ANS as well) from aqueous environment to hydrophobic environment (e.g., that of solvent-exposed hydrophobic clusters of proteins) results in a blue shift of its fluorescence maximum and in an increase of its fluorescence quantum yield (fluorescence intensity) ( [59][60][61], for review see [62]). Table 2 shows fluorescence parameters of bis-ANS bound to rat β-PA and its cluster mutants under the variety of conditions.…”