GlyProt: in silico glycosylation of proteins | Zendy

Andreas Bohne-Lang | Zendy; C.-W. von der Lieth | Zendy

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GlyProt: in silico glycosylation of proteins

Author(s) -

Andreas Bohne-Lang,

C.-W. von der Lieth

Publication year - 2005

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gki385

Subject(s) - glycan , in silico , biology , radius of gyration , glycosylation , computational biology , glycoprotein , biological system , surface (topology) , bioinformatics , biochemistry , materials science , mathematics , geometry , gene , polymer , composite material

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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