Studying the Glycan Moiety of RNase B by Means of Raman and Raman Optical Activity. Issue 11 (9th April 2014)

• Record Type: Journal Article
• Authors: Mensch, Carl; Pendrill, Robert; Widmalm, Göran; Johannessen, Christian
• Is Part Of: Chemphyschem. Volume 15:Issue 11(2014)
• Page Start: 2252
• Page End: 2254
• Publication Date: 2014-04-09
• Subjects: Chemistry, Physical and theoretical -- Periodicals; 541.05
• DOI: 10.1002/cphc.201402029
• Languages: English
• ISSNs: 1439-4235

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Raman and Raman optical activity (ROA) spectroscopy are used to study the solution‐phase structure of the glycan moiety of the protein ribonuclease B (RNase B). Spectral data of the intact glycan moiety of RNase B is obtained by subtracting high‐quality spectral data of RNase A, the non‐glycosylated form of the RNase, from the spectra of the glycoprotein. The remaining difference spectra are compared to spectra generated from Raman and ROA data of the constituent disaccharides of the RNase glycan, achieving convincing spectral overlap. The results show that ROA spectroscopy is able to extract detailed spectral data of the glycan moieties of proteins, provided that the non‐glycosylated isoform is available. Furthermore, good comparison between the full glycan spectrum and the regenerated spectra based on the disaccharide data lends great promise to ROA as a tool for the solution‐phase structural analysis of this structurally elusive class of biomolecules.</p> </abstract>