Glycan structure of a high mannose glycoprotein from raman optical activity

Johannessen, C., Pendrill, R., Widmalm, G., Hecht, L. and Barron, L. D. (2011) Glycan structure of a high mannose glycoprotein from raman optical activity. Angewandte Chemie (International Edition), 50(23), pp. 5349-5341. (doi: 10.1002/anie.201008258) (PMID:21523866)

Full text not currently available from Enlighten.

Abstract

<b>A revealing signature:</b> The glycan structure of intact yeast external invertase, a high-mannose glycoprotein used as biocatalyst, was investigated by using Raman optical activity (ROA) spectroscopy. The conformational preferences present in mannose-containing di- and trisaccharides were found to be preserved in the glycan chains, with secondary polpeptide backbone structure suppressed.

Item Type:Articles
Keywords:Glycoproteins, glycosylation, invertase, Raman optical activity
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Hecht, Dr Lutz and Barron, Professor Laurence and Johannessen, Dr Christian
Authors: Johannessen, C., Pendrill, R., Widmalm, G., Hecht, L., and Barron, L. D.
Subjects:Q Science > QD Chemistry
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Angewandte Chemie (International Edition)
Publisher:Wiley - V C H Verlag GmbH & Co. KGaA
ISSN:1433-7851
ISSN (Online):1521-3757
Published Online:26 April 2011

University Staff: Request a correction | Enlighten Editors: Update this record

Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
466991Solution structures of natural and synthetic chiral oligomers and polymers from ab initio simulations of Raman Optical Activity data.Lutz HechtEngineering & Physical Sciences Research Council (EPSRC)EP/F029713/1Chemistry