Prediction of the disulfide-bonding state of cysteines in proteins based on dipeptide composition.
In this paper, a novel approach has been introduced to predict the disulfide-bonding state of cysteines in proteins by means of a linear discriminator based on their dipeptide composition. The prediction is performed with a newly enlarged dataset with 8114 cysteine-containing segments extracted from 1856 non-homologous proteins of well-resolved three-dimensional structures. The oxidation of cysteines exhibits obvious cooperativity: almost all cysteines in disulfide-bond-containing proteins are in the oxidized form. This cooperativity can be well described by protein's dipeptide composition, based on which the prediction accuracy of the oxidation form of cysteines scores as high as 89.1% and 85.2%, when measured on cysteine and protein basis using the rigorous jack-knife procedure, respectively. The result demonstrates the applicability of this new relatively simple method and provides superior prediction performance compared with existing methods for the prediction of the oxidation states of cysteines in proteins.
Song
Jiang-Ning
JN
The Key Laboratory of Industrial Biotechnology, Ministry of Education, Southern Yangtze University, Wuxi 214036, China. sjnbeckham@yahoo.com.cn
Wang
Ming-Lei
ML
Li
Wei-Jiang
WJ
Xu
Wen-Bo
WB
D000595:Amino Acid Sequence; D003545:Cysteine / Q000737:chemistry*; D030562:Databases, Protein; D004151:Dipeptides / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D008956:Models, Chemical; D010084:Oxidation-Reduction
D004151:Dipeptides; D004220:Disulfides; D003545:Cysteine