Glycation of proteins is a nonenzymatic process in which proteins react with reducing sugar molecules. This process takes place at ε-amino (ε-NH+) groups of lysine or hydroxylysine residues as well as α-amino groups of N-terminal residues. In the present study glycation of ε-NH+ groups of lysines was computationally analyzed for 26 proteins based on their 3D structures. | Turkish Journal of Biology Turk J Biol (2016) 40: 12-25 © TÜBİTAK doi: Research Article Prediction of glycation sites: new insights from protein structural analysis 1, 2, 3 3 Homero SÁENZ-SUÁREZ *, Raúl A. POUTOU-PIÑALES *, Janneth GONZÁLEZ-SANTOS , George E. BARRETO , 4 1 5 6 Lynda P. RIETO-NAVARRERA , José A. SÁENZ-MORENO , Patricia LANDÁZURI , Luis A. BARRERA-AVELLANEDA 1 Unit of Cellular Biology and Microscopy, Dean of Health Sciences, Universidad Centroccidental Lisandro Alvarado (UCLA), Barquisimeto, Venezuela 2 Laboratory of Molecular Biotechnology, Group of Environmental and Industrial Biotechnology (GBAI), Department of Microbiology, School of Sciences, Pontificia Universidad Javeriana, Bogotá, DC Colombia 3 Group of Computational and Structural Biochemistry, Department of Biochemistry and Nutrition, School of Sciences, Pontificia Universidad Javeriana, Bogotá, DC Colombia 4 Master’s Program in Biological Sciences, School of Sciences, Pontificia Universidad Javeriana, Bogotá, DC Colombia 5 Research Group on Cardiovascular and Metabolic Diseases (GECAVYME), School of Health Sciences, Universidad del Quindío, Armenia-Quindío, Colombia 6 Institute for the Study of Inborn Errors of Metabolism (IEIM), School of Sciences, Pontificia Universidad Javeriana, Bogotá, DC Colombia Received: Accepted/Published Online: Final Version: Abstract: Glycation of proteins is a nonenzymatic process in which proteins react with reducing sugar molecules. This process takes place at ε-amino (ε-NH+) groups of lysine or hydroxylysine residues as well as α-amino groups of N-terminal residues. In the present study glycation of ε-NH+ groups of lysines was computationally analyzed for 26 proteins based on their 3D structures. We determined the spatial relationship with acidic or basic residues and correlated them with the glycation prediction algorithm Netglycate software, which .
