کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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442991 | 692450 | 2007 | 13 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Proteometric study of ghrelin receptor function variations upon mutations using amino acid sequence autocorrelation vectors and genetic algorithm-based least square support vector machines Proteometric study of ghrelin receptor function variations upon mutations using amino acid sequence autocorrelation vectors and genetic algorithm-based least square support vector machines](/preview/png/442991.png)
Functional variations on the human ghrelin receptor upon mutations have been associated with a syndrome of short stature and obesity, of which the obesity appears to develop around puberty. In this work, we reported a proteometrics analysis of the constitutive and ghrelin-induced activities of wild-type and mutant ghrelin receptors using amino acid sequence autocorrelation (AASA) approach for protein structural information encoding. AASA vectors were calculated by measuring the autocorrelations at sequence lags ranging from 1 to 15 on the protein primary structure of 48 amino acid/residue properties selected from the AAindex database. Genetic algorithm-based multilinear regression analysis (GA-MRA) and genetic algorithm-based least square support vector machines (GA-LSSVM) were used for building linear and non-linear models of the receptor activity. A genetic optimized radial basis function (RBF) kernel yielded the optimum GA-LSSVM models describing 88% and 95% of the cross-validation variance for the constitutive and ghrelin-induced activities, respectively. AASA vectors in the optimum models mainly appeared weighted by hydrophobicity-related properties. However, differently to the constitutive activity, the ghrelin-induced activity was also highly dependent of the steric features of the receptor.
Journal: Journal of Molecular Graphics and Modelling - Volume 26, Issue 1, July 2007, Pages 166–178