Incorporating significant amino acid pairs to identify O-linked glycosylation sites on transmembrane proteins and non-transmembr

Background: While occurring enzymatically in biological systems, O-linked glycosylation affects protein folding, localization and trafficking, protein solubility, antigenicity, biological activity, as well as cell-cell interactions on membrane proteins. Catalytic enzymes involve glycotransferases, sugar-transferring enzymes and glycosidases which trim specific monosaccharides from precursors to form intermediate structures. Due to the difficulty of experimental identification, several works have used computational methods to identify glycosylation sites. Results: By investigating glycosylated sites that contain various motifs between Transmembrane (TM) and nonTransmembrane (non-TM) proteins, this work presents a novel method, GlycoRBF, that implements radial basis function (RBF) networks with significant amino acid pairs (SAAPs) for identifying O-linked glycosylated serine and threonine on TM proteins and non-TM proteins. Additionally, a membrane topology is considered for reducing th...

• Type: Journal
• Year: 2010
• Where: BMCBI
• Authors: Shu-An Chen, Tzong-Yi Lee, Yu-Yen Ou
• Keywords: BMCBI 2010, Glycosylated, Proteins, TM Proteins