Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8961934 | Methods | 2018 | 17 Pages |
Abstract
Intrinsically disordered proteins (IDPs) are getting more and more interest of the scientific community. Nuclear magnetic resonance (NMR) is often a technique of choice for these studies, as it provides atomic-resolution information on structure, dynamics and interactions of IDPs. Nonetheless, NMR spectra of IDPs are typically extraordinary crowded, comparing to those of structured proteins. To overcome this problem, high-dimensional NMR experiments can be used, which allow for a better peak separation. In the present review different aspects of such experiments are discussed, from data acquisition and processing to analysis, focusing on experiments for resonance assignment.
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Authors
Katarzyna GrudziÄ
ż, Anna Zawadzka-Kazimierczuk, Wiktor KoźmiÅski,