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Studying the Glycan Moiety of RNase B by Means of Raman and Raman Optical Activity
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för organisk kemi.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för organisk kemi.
2014 (engelsk)Inngår i: ChemPhysChem, ISSN 1439-4235, E-ISSN 1439-7641, Vol. 15, nr 11, s. 2252-2254Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2014. Vol. 15, nr 11, s. 2252-2254
Emneord [en]
carbohydrates, glycoproteins, Raman optical activity, Raman spectroscopy, ribonuclease
HSV kategori
Identifikatorer
URN: urn:nbn:se:su:diva-107111DOI: 10.1002/cphc.201402029ISI: 000340175800009OAI: oai:DiVA.org:su-107111DiVA, id: diva2:743339
Forskningsfinansiär
Swedish Research Council
Merknad

AuthorCount:4;

Tilgjengelig fra: 2014-09-03 Laget: 2014-09-03 Sist oppdatert: 2017-12-05bibliografisk kontrollert

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