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Cold stability of intrinsically disordered proteins

โœ Scribed by Agnes Tantos; Peter Friedrich; Peter Tompa


Book ID
113621183
Publisher
Elsevier Science
Year
2008
Tongue
English
Weight
421 KB
Volume
583
Category
Article
ISSN
0014-5793

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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