| _version_ |
1860799705749913600
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| building |
INTELEK Repository
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| collection |
Online Access
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| collectionurl |
https://intelek.unisza.edu.my/intelek/pages/search.php?search=!collection407072
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| date |
2013-02-13 13:58:16
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| format |
Restricted Document
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| id |
7074
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| institution |
UniSZA
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| originalfilename |
2213-01-FH02-FBIM-19-25214.pdf
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| person |
Matzakaria
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| recordtype |
oai_dc
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| resourceurl |
https://intelek.unisza.edu.my/intelek/pages/view.php?ref=7074
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| spelling |
7074 https://intelek.unisza.edu.my/intelek/pages/view.php?ref=7074 https://intelek.unisza.edu.my/intelek/pages/search.php?search=!collection407072 Restricted Document Article Journal application/pdf 11 1.6 Adobe Acrobat Pro DC 20 Paper Capture Plug-in Matzakaria 2013-02-13 13:58:16 2213-01-FH02-FBIM-19-25214.pdf UniSZA Private Access In silico sequence analysis of coagulase in staphylococcus aureus Journal of agrobiotechnology Coagulase production is generally accepted as being characteristic of pathogenic and potentially pathogenic strains. Coagulase can cause clot formation in the immediate vicinity of the bacterium. The protein has been shown to contribute to bacterial virulence in wound infections owing to its ability to delay the healing processes. In this study, we conducted in silico sequence analysis using coagulase from the Gram-positive human pathogen Staphylococcus aureus with GenBank Accession no. CAC 84776.1. Various bioinformatics tools were used to predict the properties of the S. aureus coagulase. The N-terminal portion of coagulase was predicted to form transmembrane helices whereas the majority of the protein was hydrophilic in nature and was predicted to form several alpha-helices. Coagulase was also predicted to localize extracellularly and has a pI value of 8.41. The in silico analysis carried out offers an alternative way to obtain structural information and will assist in determining the structural prediction of the S. aureus coagulase 3 1 35-45
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| spellingShingle |
In silico sequence analysis of coagulase in staphylococcus aureus
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| summary |
Coagulase production is generally accepted as being characteristic of pathogenic and potentially pathogenic strains. Coagulase can cause clot formation in the immediate vicinity of the bacterium. The protein has been shown to contribute to bacterial virulence in wound infections owing to its ability to delay the healing processes. In this study, we conducted in silico sequence analysis using coagulase from the Gram-positive human pathogen Staphylococcus aureus with GenBank Accession no. CAC 84776.1. Various bioinformatics tools were used to predict the properties of the S. aureus coagulase. The N-terminal portion of coagulase was predicted to form transmembrane helices whereas the majority of the protein was hydrophilic in nature and was predicted to form several alpha-helices. Coagulase was also predicted to localize extracellularly and has a pI value of 8.41. The in silico analysis carried out offers an alternative way to obtain structural information and will assist in determining the structural prediction of the S. aureus coagulase
|
| title |
In silico sequence analysis of coagulase in staphylococcus aureus
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| title_full |
In silico sequence analysis of coagulase in staphylococcus aureus
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| title_fullStr |
In silico sequence analysis of coagulase in staphylococcus aureus
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| title_full_unstemmed |
In silico sequence analysis of coagulase in staphylococcus aureus
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| title_short |
In silico sequence analysis of coagulase in staphylococcus aureus
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| title_sort |
in silico sequence analysis of coagulase in staphylococcus aureus
|