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Assessing the Structural Ensemble and Folding Propensity of Intrinsically Disordered Proteins

โœ Scribed by Stanley, Christopher B.; Debuhr, Amanda; Grese, Laura; Rowe, Erica; O'Neill, Hugh; Berthelier, Valerie


Book ID
122156393
Publisher
Biophysical Society
Year
2012
Tongue
English
Weight
52 KB
Volume
102
Category
Article
ISSN
0006-3495

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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