Structural analysis and modeling comparison of primates’ amyloid ßa4 protein

Amyloid protein originally termed "beta-protein" or "amyloid A4" which is indicated as "beta A4." Amyloid beta A4 protein is proteolytically derived from a transmembrane protein named amyloid precursor protein (APP) which is encoded by an extensively expressed gene on c...

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Main Author: Jalali, Fahimeh
Format: Thesis
Language:English
Published: 2013
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Online Access:http://eprints.utm.my/id/eprint/40534/5/FahimehJalaliMFBB2013.pdf
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spelling my-utm-ep.405342017-09-11T08:41:30Z Structural analysis and modeling comparison of primates’ amyloid ßa4 protein 2013-01 Jalali, Fahimeh Q Science (General) Amyloid protein originally termed "beta-protein" or "amyloid A4" which is indicated as "beta A4." Amyloid beta A4 protein is proteolytically derived from a transmembrane protein named amyloid precursor protein (APP) which is encoded by an extensively expressed gene on chromosome 21. Mutations in Amyloid ßA4 gene cause the plaques which are composed of a tangle of regularly ordered fibrillar aggregates called amyloid fibers, and abnormal accumulation of amyloid fibrils make protein misfolding diseases so that it leads to amyloidosis and neurodegenerative disorder like Alzheimer diseases (AD) or Parkinson diseases (PD).Currently there are 91 structure of Amyloid beta A4 protein have been predicted in various species, but there is no presently concrete evidence that shows Amyloid beta A4 model in primates. This study was focus on Amyloid beta A4 protein information and analyzed using bioinformatics software such as: Uniprot, Deep View, PDB (protein data bank), Swiss Model, Jal View, BLAST, VMD(Visual molecular dynamics), NCBI(National center for biotechnology information) therefore those of programs help us to predict and create a new model of 3D structure for this protein and they are useful for analysis multiple alignment, simulation , image processing for ßA4 protein sequence, illustrate conserved regions and residues of protein between different species (human being and primates) to indicate comparison of their structural features and their gen properties to this end 8 primates were chosen. Based on the analysis of this comparison demonstrated that some of the primates are highly conserved with their template (Homo sapiens) and they have similar primary and tertiary structure with template .The reason of this issue is that in all of them the protein’s gene location is on chromosome 21 as same as human gen location. On the other hand rest of chosen primates is not conserved with template and their structures are totally different with Homo sapiens due to APP gene location is on chromosome 3 instead of chromosome 21. This information was gathered from GenBank which is the genetic sequence database, an annotated collection of all publicly available DNA sequences 2013-01 Thesis http://eprints.utm.my/id/eprint/40534/ http://eprints.utm.my/id/eprint/40534/5/FahimehJalaliMFBB2013.pdf application/pdf en public masters Universiti Teknologi Malaysia, Faculty of Biosciences and Bioengineering Faculty of Biosciences and Bioengineering
institution Universiti Teknologi Malaysia
collection UTM Institutional Repository
language English
topic Q Science (General)
spellingShingle Q Science (General)
Jalali, Fahimeh
Structural analysis and modeling comparison of primates’ amyloid ßa4 protein
description Amyloid protein originally termed "beta-protein" or "amyloid A4" which is indicated as "beta A4." Amyloid beta A4 protein is proteolytically derived from a transmembrane protein named amyloid precursor protein (APP) which is encoded by an extensively expressed gene on chromosome 21. Mutations in Amyloid ßA4 gene cause the plaques which are composed of a tangle of regularly ordered fibrillar aggregates called amyloid fibers, and abnormal accumulation of amyloid fibrils make protein misfolding diseases so that it leads to amyloidosis and neurodegenerative disorder like Alzheimer diseases (AD) or Parkinson diseases (PD).Currently there are 91 structure of Amyloid beta A4 protein have been predicted in various species, but there is no presently concrete evidence that shows Amyloid beta A4 model in primates. This study was focus on Amyloid beta A4 protein information and analyzed using bioinformatics software such as: Uniprot, Deep View, PDB (protein data bank), Swiss Model, Jal View, BLAST, VMD(Visual molecular dynamics), NCBI(National center for biotechnology information) therefore those of programs help us to predict and create a new model of 3D structure for this protein and they are useful for analysis multiple alignment, simulation , image processing for ßA4 protein sequence, illustrate conserved regions and residues of protein between different species (human being and primates) to indicate comparison of their structural features and their gen properties to this end 8 primates were chosen. Based on the analysis of this comparison demonstrated that some of the primates are highly conserved with their template (Homo sapiens) and they have similar primary and tertiary structure with template .The reason of this issue is that in all of them the protein’s gene location is on chromosome 21 as same as human gen location. On the other hand rest of chosen primates is not conserved with template and their structures are totally different with Homo sapiens due to APP gene location is on chromosome 3 instead of chromosome 21. This information was gathered from GenBank which is the genetic sequence database, an annotated collection of all publicly available DNA sequences
format Thesis
qualification_level Master's degree
author Jalali, Fahimeh
author_facet Jalali, Fahimeh
author_sort Jalali, Fahimeh
title Structural analysis and modeling comparison of primates’ amyloid ßa4 protein
title_short Structural analysis and modeling comparison of primates’ amyloid ßa4 protein
title_full Structural analysis and modeling comparison of primates’ amyloid ßa4 protein
title_fullStr Structural analysis and modeling comparison of primates’ amyloid ßa4 protein
title_full_unstemmed Structural analysis and modeling comparison of primates’ amyloid ßa4 protein
title_sort structural analysis and modeling comparison of primates’ amyloid ßa4 protein
granting_institution Universiti Teknologi Malaysia, Faculty of Biosciences and Bioengineering
granting_department Faculty of Biosciences and Bioengineering
publishDate 2013
url http://eprints.utm.my/id/eprint/40534/5/FahimehJalaliMFBB2013.pdf
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