Computational Analysis of Heat shock Protein 27 (HSP27) from different source organisms
Heat shock protein 27 (HSP27) also called HSPB1 is a member of small heat shock protein (sHsps). HSB1 helps in developing a stable state during stress conditions like heat shock or oxidative injuries. Several studies have performed for the identification of HSPB1 function. However, limitation to hig...
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ftvfastojs:oai:ojs.localhost:article/859 2023-05-15T15:49:37+02:00 Computational Analysis of Heat shock Protein 27 (HSP27) from different source organisms Afzal, Urwa Bukhari, Sarah Pervez, Muhammad Tariq Aslam, Naeem 2022-02-07 application/pdf https://vfast.org/journals/index.php/VTSE/article/view/859 https://doi.org/10.21015/vtse.v10i1.859 eng eng VFAST Transactions on Software Engineering https://vfast.org/journals/index.php/VTSE/article/view/859/804 https://vfast.org/journals/index.php/VTSE/article/view/859 doi:10.21015/vtse.v10i1.859 Authors who publish with this journal agree to the following terms:Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License (CC-By) that allows others to share the work with an acknowledgment of the work's authorship and initial publication in this journal.Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access). This work is licensed under a Creative Commons Attribution License CC BY VFAST Transactions on Software Engineering; Vol 10, No 1 (2022): January-March; 1-16 2309-3978 2411-6246 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Peer-reviewed Article 2022 ftvfastojs https://doi.org/10.21015/vtse.v10i1.859 2023-04-10T05:30:07Z Heat shock protein 27 (HSP27) also called HSPB1 is a member of small heat shock protein (sHsps). HSB1 helps in developing a stable state during stress conditions like heat shock or oxidative injuries. Several studies have performed for the identification of HSPB1 function. However, limitation to highlight structural and phylogenetic relationships of HSPB1 in various organisms. Therefore, the aim of this study to investigate HSPB1 protein in twelve different organisms namely Homo Sapiens (Human), Dugesia japonica (Flatworms), Sus scrofa (Pig), Carassius auratus (Goldfish), Oreochromis niloticus (Nile Tilapia), Rattus norvegicus (Norway Rat), Xenopus laevis (African clawed Frog), Canis lupus familiaris (Dog), Musca domestica (House Fly), Phenacoccus solenopsis (Solenopsis mealybug), Kryptolebias marmoratus (mangrove rivulus\fish) and Alligator mississippiensis (American alligator) by identifying and analyzing the Multiple sequence alignment (MSA), similarity matrix, physiochemical properties, phylogenetic relationship, secondary and tertiary structure, predict motifs and domains, analyze gene structure through several tools.For this purpose organisms were predicted based on soluble and hydrophilic in nature.Results showed all organisms had upstream, downstream and CDS part in their protein sequences except Kryptolebias marmoralus (fish), Oreochromis Niloticus (Nile Tilapia),Phenacoccus Solenopsis (Solenopsis mealybug), and Sus Scrofa (Pig) which had only CDS part. The main domain that was found in all organisms except Phenacoccus were A-Crystalline(IPR002068) and the homologous super family in all organisms were Hsp20 (IPR002068).In phylogenetic tree two clades formed and in the endidentified that Rattus norvegicus and Canis lupus are more similar with each other as they share many common features. Moreover Homo Sapiens, Sus scrofa and Canis lupus, Sus scrofa were found to be more similar. By performing different analysis it was predicted that Phenacoccus Solenopsis was not related to any organism in many aspects. ... Article in Journal/Newspaper Canis lupus VFAST - Virtual Foundation for Advancement of Science and Technology (Pakistan) Norway |
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Open Polar |
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VFAST - Virtual Foundation for Advancement of Science and Technology (Pakistan) |
op_collection_id |
ftvfastojs |
language |
English |
description |
Heat shock protein 27 (HSP27) also called HSPB1 is a member of small heat shock protein (sHsps). HSB1 helps in developing a stable state during stress conditions like heat shock or oxidative injuries. Several studies have performed for the identification of HSPB1 function. However, limitation to highlight structural and phylogenetic relationships of HSPB1 in various organisms. Therefore, the aim of this study to investigate HSPB1 protein in twelve different organisms namely Homo Sapiens (Human), Dugesia japonica (Flatworms), Sus scrofa (Pig), Carassius auratus (Goldfish), Oreochromis niloticus (Nile Tilapia), Rattus norvegicus (Norway Rat), Xenopus laevis (African clawed Frog), Canis lupus familiaris (Dog), Musca domestica (House Fly), Phenacoccus solenopsis (Solenopsis mealybug), Kryptolebias marmoratus (mangrove rivulus\fish) and Alligator mississippiensis (American alligator) by identifying and analyzing the Multiple sequence alignment (MSA), similarity matrix, physiochemical properties, phylogenetic relationship, secondary and tertiary structure, predict motifs and domains, analyze gene structure through several tools.For this purpose organisms were predicted based on soluble and hydrophilic in nature.Results showed all organisms had upstream, downstream and CDS part in their protein sequences except Kryptolebias marmoralus (fish), Oreochromis Niloticus (Nile Tilapia),Phenacoccus Solenopsis (Solenopsis mealybug), and Sus Scrofa (Pig) which had only CDS part. The main domain that was found in all organisms except Phenacoccus were A-Crystalline(IPR002068) and the homologous super family in all organisms were Hsp20 (IPR002068).In phylogenetic tree two clades formed and in the endidentified that Rattus norvegicus and Canis lupus are more similar with each other as they share many common features. Moreover Homo Sapiens, Sus scrofa and Canis lupus, Sus scrofa were found to be more similar. By performing different analysis it was predicted that Phenacoccus Solenopsis was not related to any organism in many aspects. ... |
format |
Article in Journal/Newspaper |
author |
Afzal, Urwa Bukhari, Sarah Pervez, Muhammad Tariq Aslam, Naeem |
spellingShingle |
Afzal, Urwa Bukhari, Sarah Pervez, Muhammad Tariq Aslam, Naeem Computational Analysis of Heat shock Protein 27 (HSP27) from different source organisms |
author_facet |
Afzal, Urwa Bukhari, Sarah Pervez, Muhammad Tariq Aslam, Naeem |
author_sort |
Afzal, Urwa |
title |
Computational Analysis of Heat shock Protein 27 (HSP27) from different source organisms |
title_short |
Computational Analysis of Heat shock Protein 27 (HSP27) from different source organisms |
title_full |
Computational Analysis of Heat shock Protein 27 (HSP27) from different source organisms |
title_fullStr |
Computational Analysis of Heat shock Protein 27 (HSP27) from different source organisms |
title_full_unstemmed |
Computational Analysis of Heat shock Protein 27 (HSP27) from different source organisms |
title_sort |
computational analysis of heat shock protein 27 (hsp27) from different source organisms |
publisher |
VFAST Transactions on Software Engineering |
publishDate |
2022 |
url |
https://vfast.org/journals/index.php/VTSE/article/view/859 https://doi.org/10.21015/vtse.v10i1.859 |
geographic |
Norway |
geographic_facet |
Norway |
genre |
Canis lupus |
genre_facet |
Canis lupus |
op_source |
VFAST Transactions on Software Engineering; Vol 10, No 1 (2022): January-March; 1-16 2309-3978 2411-6246 |
op_relation |
https://vfast.org/journals/index.php/VTSE/article/view/859/804 https://vfast.org/journals/index.php/VTSE/article/view/859 doi:10.21015/vtse.v10i1.859 |
op_rights |
Authors who publish with this journal agree to the following terms:Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License (CC-By) that allows others to share the work with an acknowledgment of the work's authorship and initial publication in this journal.Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access). This work is licensed under a Creative Commons Attribution License CC BY |
op_doi |
https://doi.org/10.21015/vtse.v10i1.859 |
_version_ |
1766384657143693312 |