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Updated: May 17, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Detection of disordered regions in globular proteins using ¹³C-detected NMR
Felicia L V Gray1, Marcelo J Murai, Jolanta Grembecka
1Department of Pathology, University of Michigan, Ann Arbor, Michigan 48109, USA.
Abstract:
Characterization of disordered regions in globular proteins constitutes a significant challenge. Here, we report an approach based on ¹³C-detected nuclear magnetic resonance experiments for the identification and assignment of disordered regions in large proteins. Using this method, we demonstrate that disordered fragments can be accurately identified in two homologs of menin, a globular protein with a molecular weight over 50 kDa. Our work provides an efficient way to characterize disordered fragments in globular proteins for structural biology applications.
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