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
โฆ LIBER โฆ
Structure and Function of Intrinsically Disordered Proteins. By Peter Tompa.
โ Scribed by Edward A. Lemke
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 73 KB
- Volume
- 12
- Category
- Article
- ISSN
- 1439-4227
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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