𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Charge-Induced Molecular Alignment of Intrinsically Disordered Proteins

✍ Scribed by Lukasz Skora; Min-Kyu Cho; Hai-Young Kim; Stefan Becker; Claudio O. Fernandez; Martin Blackledge; Markus Zweckstetter

Publisher
John Wiley and Sons
Year
2006
Tongue
English
Weight
325 KB
Volume
45
Category
Article
ISSN
0044-8249

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Limitations of Induced Folding in Molecu
Limitations of Induced Folding in Molecular Recognition by Intrinsically Disordered Proteins
✍ Eszter Hazy; Peter Tompa πŸ“‚ Article πŸ“… 2009 πŸ› John Wiley and Sons 🌐 English βš– 212 KB

## Abstract **Intrinsically disordered proteins** exist and function without well‐defined three‐dimensional structures and are common in proteomes where they carry out essential functions. Herein, evidence for their lack of structure and the major functional benefits that this confers, are surveyed

Instrumental Analysis of Intrinsically D
Instrumental Analysis of Intrinsically Disordered Proteins (Assessing Structure and Conformation) || Fluorescence Spectroscopy of Intrinsically Disordered Proteins
✍ Uversky, Vladimir N.; Longhi, Sonia πŸ“‚ Article πŸ“… 2010 πŸ› John Wiley & Sons, Inc. 🌐 English βš– 350 KB πŸ‘ 1 views

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