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Updated: Jul 5, 2026

12:47
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Studying posttranslational modifications by in-cell NMR
G Lippens1, I Landrieu, X Hanoulle
1CNRS-USTL UMR 8576, Structural and Functional Glycobiology, University of Lille I, 59655 Villeneuve d'Ascq, France. Guy.Lippens@univ-lille1.fr
Chemistry & Biology
|April 19, 2008
Abstract:
Functional in vivo investigation of posttranslational modifications is a problem that a number of analytical techniques are trying to tackle. Below, we briefly discuss the breakthroughs and challenges in placing NMR spectroscopy on the map, as illustrated by a recent report by Selenko et al. (2008).
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Applications Of NMR In Biology
Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
The...
The...
Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

