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GlyProt: in silico glycosylation of proteins

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 radiu...

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Detalles Bibliográficos
Autores principales: Bohne-Lang, Andreas, von der Lieth, Claus-Wilhelm
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1160146/
https://www.ncbi.nlm.nih.gov/pubmed/15980456
http://dx.doi.org/10.1093/nar/gki385
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author Bohne-Lang, Andreas
von der Lieth, Claus-Wilhelm
author_facet Bohne-Lang, Andreas
von der Lieth, Claus-Wilhelm
author_sort Bohne-Lang, Andreas
collection PubMed
description 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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spelling pubmed-11601462005-06-29 GlyProt: in silico glycosylation of proteins Bohne-Lang, Andreas von der Lieth, Claus-Wilhelm Nucleic Acids Res Article 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. Oxford University Press 2005-07-01 2005-06-27 /pmc/articles/PMC1160146/ /pubmed/15980456 http://dx.doi.org/10.1093/nar/gki385 Text en © The Author 2005. Published by Oxford University Press. All rights reserved
spellingShingle Article
Bohne-Lang, Andreas
von der Lieth, Claus-Wilhelm
GlyProt: in silico glycosylation of proteins
title GlyProt: in silico glycosylation of proteins
title_full GlyProt: in silico glycosylation of proteins
title_fullStr GlyProt: in silico glycosylation of proteins
title_full_unstemmed GlyProt: in silico glycosylation of proteins
title_short GlyProt: in silico glycosylation of proteins
title_sort glyprot: in silico glycosylation of proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1160146/
https://www.ncbi.nlm.nih.gov/pubmed/15980456
http://dx.doi.org/10.1093/nar/gki385
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