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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1160146 | PMC |
| http://dx.doi.org/10.1093/nar/gki385 | DOI Listing |
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In silico design and analysis of a new hyperglycosylated analog of erythropoietin to improve drug efficacy.
Adv Biomed Res
August 2015
Biochemistry Department, Genetic and Metabolism Research Group, Pasteur Institute of Iran, Tehran.
Background: The enhancement of glycosylation by applying glycoengineering approaches has become widely used to boost properties for protein therapeutics. The objective of this work was to engineer a new hyperglycosylated analog of erythropoietin (EPO) with appropriately targeted N-linked carbohydrates through bioinformatics tools.
Materials And Methods: The EPO protein sequence was retrieved from NCBI protein sequence database.
GlyProt: in silico glycosylation of proteins.
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German Cancer Research Center Heidelberg, Central Spectroscopy-Molecular Modeling Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.
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.
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