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Issue 10, 2007
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Quantification of casein phosphorylation with conformational interpretation using Raman spectroscopy

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Abstract

Raman spectroscopy is emerging as a powerful method for obtaining both quantitative and qualitative information from biological samples. One very interesting area of research, for which the technique has rarely been used, is the detection, quantification and structural analysis of post-translational modifications (PTMs) on proteins. Since Raman spectra can be used to address both of these questions simultaneously, we have developed near infrared Raman spectroscopy with appropriate chemometric approaches (partial least squares regression) to quantify low concentration (4 µM) mixtures of phosphorylated and dephosphorylated bovine αs-casein. In addition, we have used these data in conjunction with Raman optical activity (ROA) spectra and NMR to assess the structural changes that occur upon phosphorylation.

Graphical abstract: Quantification of casein phosphorylation with conformational interpretation using Raman spectroscopy

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Publication details

The article was received on 27 Feb 2007, accepted on 16 Jul 2007 and first published on 07 Aug 2007


Article type: Paper
DOI: 10.1039/B702944F
Citation: Analyst, 2007,132, 1053-1060
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    Quantification of casein phosphorylation with conformational interpretation using Raman spectroscopy

    R. M. Jarvis, E. W. Blanch, A. P. Golovanov, J. Screen and R. Goodacre, Analyst, 2007, 132, 1053
    DOI: 10.1039/B702944F

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