Computational approaches for structure-based molecular characterization and functional annotation of the fusion protein of nipah henipavirus “2279

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SUMMARY

    The selected protein for this study is a fusion_protein of Nipah henipavirus, which is associated with viral infections. The protein sequence retrieved from the NCBI database contains 546 amino_acid residues. The physicochemical parameters of a protein are defined by the characteristics of its constituent amino_acids. The alpha-carbon unit of all amino_acids, except for glycine, is asymmetric, indicating that it is connected to four distinct chemical constituents (atoms or atom pairs). Leucine is the most abundant amino_acid (61, 11.2%) compared 3 of 10 to others in the amino_acid sequence. Hydrophobicity is a property . . .

     

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