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Instrumental Analysis of Intrinsically Disordered Proteins (Assessing Structure and Conformation) || The Structural Biology of IDPs inside Cells

โœ Scribed by Uversky, Vladimir N.; Longhi, Sonia

Publisher
John Wiley & Sons, Inc.
Year
2010
Tongue
English
Weight
211 KB
Edition
1
Category
Article
ISBN
0470343419

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The degradation of the majority of cellular proteins is mediated by the proteasomes. Ubiquitin -dependent proteasomal protein degradation is executed by a number of enzymes that interact to modify the substrates prior to their engagement with the 26S proteasomes. The 26S proteasome is made of two co

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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