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Nucleic Acids Research 2005 33(Web Server Issue):W214-W219; doi:10.1093/nar/gki385
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© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

GlyProt: in silico glycosylation of proteins

Andreas Bohne-Lang* and Claus-Wilhelm von der Lieth

German Cancer Research Center Heidelberg, Central Spectroscopy–Molecular Modeling Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany

*To whom correspondence should be addressed. Tel: +49 6221 42 4541; Fax: +49 6221 42 3669; Email: a.bohne{at}dkfz-heidelberg.de

Received February 11, 2005. Revised March 9, 2005. Accepted March 9, 2005.

GlyProt (http://www.glycosciences.de/glyprot/) is a web-based tool that enables meaningful N-glycan conformations to be attached to all the spatially accessible potential N-glycosylation sites of a known three-dimensional (3D) protein structure. The probabilities of physicochemical properties such as mass, accessible surface and radius of gyration are calculated. The purpose of this service is to provide rapid access to reliable 3D models of glycoproteins, which can subsequently be refined by using more elaborate simulations and validated by comparing the generated models with experimental data.


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