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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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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2005
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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. |
format | Text |
id | pubmed-1160146 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT bohnelangandreas glyprotinsilicoglycosylationofproteins AT vonderliethclauswilhelm glyprotinsilicoglycosylationofproteins |