1,720,963 research outputs found
Total energy and RMSD of deleterious nsSNPs.
No full textTotal energy and RMSD of deleterious nsSNPs.</p
Comparing the helix, protein binding, Disordered region and exposed/buried residues.
No full textComparing the helix, protein binding, Disordered region and exposed/buried residues.</p
Cumulative prediction of possible deleterious nsSNPs.
No full textCumulative prediction of possible deleterious nsSNPs.</p
Prediction matching to the highly pathogenic nsSNPs of <i>HBA1</i> gene.
No full textThe 2 highly pathogenic nsSNPs are having the scores: Polyphen >0.9; Panther >0.55; SNPs&Go >0.8; SIFT = 0; PROVEAN 65.</p
Molecular dynamic simulation of native and mutant HBA1.
No full textMolecular dynamic simulation of native and mutant HBA1.</p
Graphic illustration of bioinformatic tools used for the precise identification of the most deleterious nsSNPs of <i>HBA1</i> gene.
No full textGraphic illustration of bioinformatic tools used for the precise identification of the most deleterious nsSNPs of HBA1 gene.</p
A: Comparing the secondary structure of the mutated and native HBA1 protein. B: Ramachandran plot of constructed HBA1 protein. Most of the amino acid residues were in the most favored region. C: Protein binding regions in the secondary structure of HBA1 protein. D: States of the secondary structure. E: Eight class Secondary structure of HBA1 protein by RaptorX.
No full textA: Comparing the secondary structure of the mutated and native HBA1 protein. B: Ramachandran plot of constructed HBA1 protein. Most of the amino acid residues were in the most favored region. C: Protein binding regions in the secondary structure of HBA1 protein. D: States of the secondary structure. E: Eight class Secondary structure of HBA1 protein by RaptorX.</p
Super imposed 3D structures of the native and highly deleterious mutated HBA1 proteins.
No full textSuper imposed 3D structures of the native and highly deleterious mutated HBA1 proteins.</p
In-Silico Computing of the Most Deleterious nsSNPs in HBA1 Gene.
No full textBackgroundα-Thalassemia (α-thal) is a genetic disorder caused by the substitution of single amino acid or large deletions in the HBA1 and/or HBA2 genes.MethodUsing modern bioinformatics tools as a systematic in-silico approach to predict the deleterious SNPs in the HBA1 gene and its significant pathogenic impact on the functions and structure of HBA1 protein was predicted.Results and discussionA total of 389 SNPs in HBA1 were retrieved from dbSNP database, which includes: 201 non-coding synonymous (nsSNPs), 43 human active SNPs, 16 intronic SNPs, 11 mRNA 3' UTR SNPs, 9 coding synonymous SNPs, 9 5' UTR SNPs and other types. Structural homology-based method (PolyPhen) and sequence homology-based tool (SIFT), SNPs&Go, PROVEAN and PANTHER revealed that 2.4% of the nsSNPs are pathogenic.ConclusionsA total of 5 nsSNPs (G60V, K17M, K17T, L92F and W15R) were predicted to be responsible for the structural and functional modifications of HBA1 protein. It is evident from the deep comprehensive in-silico analysis that, two nsSNPs such as G60V and W15R in HBA1 are highly deleterious. These "2 pathogenic nsSNPs" can be considered for wet-lab confirmatory analysis
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