作者: Sen Gupta , Bandyopadhyay Amal Kumar , Parth Sarthi , Banerjee Shyamashree
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摘要: In silico characterizat ion and molecular modeling of a protein opens wide scope for the prediction structural functional information. It is most significant helpful when very little information about three dimensional (3D) structure protein(uncharacterized) availab le in Protein Data Bank (PDB). So, present study has been undertaken to carried out function Ho mogentisate-1,2-dio xygenase homo sapiens. Primary analysis reveals that all six sequences Homogentisate-1,2-dio are hydrophobic nature (due high content non- polar residues) without transmemb rane region. The aliphatic index co mputation infers mogentisate-1,2-d io sapiens can't tolerate range temperature. Secondary shows have predominant sheet random coil structure. Sub cellu lar localizat predict suggested secretory transit peptide. 3D predicted characterized. Energy min imization, Refinement validation done, which suggest be good quality. model generated fo r successfully submitted Model Database (PMDB) having PMID PM0079008. Active site structure, disorder, disorder propensity Average Area Buried Upon Folding also analyzed. Fold motif predicted. This highlights sequence, formation protein.