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Updated: Jul 11, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Published on: December 27, 2016

Quantification of casein phosphorylation with conformational interpretation using Raman spectroscopy.

Roger M Jarvis¹, Ewan W Blanch, Alexander P Golovanov

¹Manchester Interdisciplinary Biocentre, 131 Princess Street, Manchester, UKM1 7ND. roger.jarvis@manchester.ac.uk

|September 26, 2007

Summary

Near-infrared Raman spectroscopy can quantify low concentrations of protein post-translational modifications (PTMs). This technique, combined with chemometrics, also assesses structural changes upon phosphorylation.

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Area of Science:

Biochemistry
Spectroscopy
Protein analysis

Background:

Raman spectroscopy offers quantitative and qualitative analysis of biological samples.
Post-translational modifications (PTMs) on proteins are crucial but challenging to analyze.
Raman spectroscopy has been underutilized for PTM detection and structural analysis.

Purpose of the Study:

To develop and apply near-infrared Raman spectroscopy for PTM detection and quantification.
To quantify low concentrations of phosphorylated and dephosphorylated bovine alpha(s)-casein.
To assess protein structural changes upon phosphorylation using Raman spectroscopy, Raman optical activity (ROA), and NMR.

Main Methods:

Near-infrared Raman spectroscopy
Chemometric approaches, including partial least squares regression
Raman optical activity (ROA) and Nuclear Magnetic Resonance (NMR) spectroscopy

Main Results:

Successfully quantified low concentration (4 microM) mixtures of phosphorylated and dephosphorylated bovine alpha(s)-casein.
Demonstrated the ability of Raman spectroscopy to simultaneously detect and quantify PTMs.
Utilized combined spectroscopic data to assess phosphorylation-induced structural alterations.

Conclusions:

Near-infrared Raman spectroscopy is a viable method for PTM quantification in biological samples.
This approach enables simultaneous qualitative and quantitative analysis of PTMs.
Integration with ROA and NMR provides insights into phosphorylation-related structural dynamics.