Instrumental Analysis of Intrinsically Disordered Proteins (Assessing Structure and Conformation) || Fluorescence Spectroscopy of Intrinsically Disordered Proteins

✍ Scribed by Uversky, Vladimir N.; Longhi, Sonia

• Publisher: John Wiley & Sons, Inc.
• Year: 2010
• Tongue: English
• Weight: 350 KB
• Edition: 1
• Category: Article
• ISBN: 0470343419
• DOI: 10.1002/9780470602614.ch11

✦ Synopsis

Fluorescence 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.