Indian Journal of Bioinformatics and Biotechnology

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Sequence and Homology Modeling Analysis of Alkaline Protease From Bacillus Sp


Affiliations
1 Dept. of Microbiology, Jessore University of Science and Technology, Bangladesh
 

Objectives: This study has been focused on the functional analysis and structure prediction of alkaline protease.

Methods: The study was performed on alkaline protease, sequence of which was taken from NCBI. The study includes functional sites analysis, physicochemical properties analysis, secondary structure and three dimensional structure predictions along with its validation.The Solvent Accessible Surface Area (SASA) of the protein was also measured. All these analysis and predictions were carried out using various computational tools.

Findings: These tools showed that the protein has 25 functional sites including myristoylation site, phosphorylation site, and glycosylation sites. It was found that the protein is stable, thermos table, hydrophobic/membranous and intracellular. 31.28% random coil structure confirms its flexibility while rest of the protein has its regular structure,confirming the stability of the protein. All of the validation results support that the predicted model of the protein was reliable.

Application: The study will be helpful for further research in signal transduction,intrinsic biological functions, and protein-protein/protein-ligand interaction and for designing new drug against it.


Keywords

Bacillus, Alkaline Protease, Homology Modeling, SASA, Subtilisin, Myristoylation.
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  • Sequence and Homology Modeling Analysis of Alkaline Protease From Bacillus Sp

Abstract Views: 598  |  PDF Views: 269

Authors

Jahangir Alam
Dept. of Microbiology, Jessore University of Science and Technology, Bangladesh

Abstract


Objectives: This study has been focused on the functional analysis and structure prediction of alkaline protease.

Methods: The study was performed on alkaline protease, sequence of which was taken from NCBI. The study includes functional sites analysis, physicochemical properties analysis, secondary structure and three dimensional structure predictions along with its validation.The Solvent Accessible Surface Area (SASA) of the protein was also measured. All these analysis and predictions were carried out using various computational tools.

Findings: These tools showed that the protein has 25 functional sites including myristoylation site, phosphorylation site, and glycosylation sites. It was found that the protein is stable, thermos table, hydrophobic/membranous and intracellular. 31.28% random coil structure confirms its flexibility while rest of the protein has its regular structure,confirming the stability of the protein. All of the validation results support that the predicted model of the protein was reliable.

Application: The study will be helpful for further research in signal transduction,intrinsic biological functions, and protein-protein/protein-ligand interaction and for designing new drug against it.


Keywords


Bacillus, Alkaline Protease, Homology Modeling, SASA, Subtilisin, Myristoylation.

References