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Studying the Glycan Moiety of RNase B by Means of Raman and Raman Optical Activity
Stockholm University, Faculty of Science, Department of Organic Chemistry.
Stockholm University, Faculty of Science, Department of Organic Chemistry.
2014 (English)In: ChemPhysChem, ISSN 1439-4235, E-ISSN 1439-7641, Vol. 15, no 11, 2252-2254 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2014. Vol. 15, no 11, 2252-2254 p.
Keyword [en]
carbohydrates, glycoproteins, Raman optical activity, Raman spectroscopy, ribonuclease
National Category
Chemical Sciences Physical Sciences
URN: urn:nbn:se:su:diva-107111DOI: 10.1002/cphc.201402029ISI: 000340175800009OAI: diva2:743339
Swedish Research Council


Available from: 2014-09-03 Created: 2014-09-03 Last updated: 2016-10-18Bibliographically approved

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