Publication
Title
Studying the glycan moiety of RNase B by means of Raman and Raman optical activity
Author
Abstract
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.
Language
English
Source (journal)
ChemPhysChem : a European journal of chemical physics and physical chemistry. - Weinheim, 2000 - 2015
Publication
Weinheim : Wiley-VCH , 2014
ISSN
1439-4235 [print]
1439-7641 [online]
DOI
10.1002/CPHC.201402029
Volume/pages
15 :11 (2014) , p. 2252-2254
ISI
000340175800009
Full text (Publisher's DOI)
UAntwerpen
Faculty/Department
Research group
Project info
Unravelling structural motives of intrinsically unstructured proteins employing Raman optical activity: Understanding the basis of neurodegenerative diseases
4D Protein Structure.
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identifier
Creation 08.09.2014
Last edited 09.10.2023
To cite this reference