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Computational Analysis of Proteases Domains using Hidden Markov Model
- Source :
- International Journal of Computer Applications. 43:32-35
- Publication Year :
- 2012
- Publisher :
- Foundation of Computer Science, 2012.
-
Abstract
- paper, we present a three-layered predictor, Profinder, for identification and analysis of protein enzyme "Protease". This predictor is shaped by collecting the protease family domains represented by multiple sequence alignments and hidden morkov modeling techniques. Present study here is an attempt to develop a specific algorithm for searching particular domains in the genome sequences of these protein enzymes. Therefore, it is important for both basic research and drug discovery to consider the following two problems. Given the sequence of a protein, determine whether the protein is a protease or not? And if so, then which class of proteases? It is only on the basis of their sequence analysis, one can identify their types and also can predict their secondary or tertiary structures. User can test their sequences in fasta format for identification of proteases domain and therefore can get some insights on their fuctions and secondary structures. Besides, analysis based on phylogenetic relation of these proteases by constructing their phylogenetic trees in the light of evolution can be done. Storing all the information extracted from these sequences in a new database is another perspective of this present in-silico study.
- Subjects :
- chemistry.chemical_classification
Proteases
Protease
Phylogenetic tree
Sequence analysis
Computer science
Drug discovery
medicine.medical_treatment
FASTA format
food and beverages
A protein
Computational biology
Bioinformatics
Genome
Enzyme
chemistry
medicine
Identification (biology)
Hidden Markov model
Sequence (medicine)
Subjects
Details
- ISSN :
- 09758887
- Volume :
- 43
- Database :
- OpenAIRE
- Journal :
- International Journal of Computer Applications
- Accession number :
- edsair.doi...........208d6dbe03316c2d04aa2c0ca7637188
- Full Text :
- https://doi.org/10.5120/6117-8317