Structural analysis and modeling comparison of primates dystrophin

Dystrophin is a rod-shaped cytoplasmic protein which is an essential piece ofa protein complex that binds the cytoskeleton of a muscle fiber to the nearby extracellular matrix within the cell membrane. Lack of this protein in the muscle leads muscular dystrophy. Currently, Dystrophin structure has j...

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Main Author: Mohajer, Faeze Sadat
Format: Thesis
Language:English
Published: 2013
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Online Access:http://eprints.utm.my/id/eprint/33293/1/FaezeSadatMohajerMFBME2013.pdf
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spelling my.utm.332932017-07-06T01:18:58Z http://eprints.utm.my/id/eprint/33293/ Structural analysis and modeling comparison of primates dystrophin Mohajer, Faeze Sadat Unspecified Dystrophin is a rod-shaped cytoplasmic protein which is an essential piece ofa protein complex that binds the cytoskeleton of a muscle fiber to the nearby extracellular matrix within the cell membrane. Lack of this protein in the muscle leads muscular dystrophy. Currently, Dystrophin structure has just been detected in human being. In fact, it has not been recognized in other types of primates. However, bioinformatics’ software has presented a big opportunity to predict its structure in other species on based on its structure in human being. The data for this project will be sourced by both bioinformatics databases and experimental information. The used databases were NCBI, PDB (protein data bank), UniProt, and Gene bank. The data that is gathered from these databases were analyzed using multiple sequence analysis software such as BLAST, Jalview to find conserved regions in the protein among the species of interest (different kinds of primates). In addition, the tertiary structure of the protein will be predicted by Swiss-model and will be observed and compared by 3-d structure viewing software such as: VMD and DeepView. In conclusion, the analysis of this study illustrates that Dystrophin has been changed slightly through evolution. However, the small changes that have been occurred have not affected the 3D structure and function of the protein. 2013 Thesis NonPeerReviewed application/pdf en http://eprints.utm.my/id/eprint/33293/1/FaezeSadatMohajerMFBME2013.pdf Mohajer, Faeze Sadat (2013) Structural analysis and modeling comparison of primates dystrophin. Masters thesis, Universiti Teknologi Malaysia, Faculty of Biosciences and Medical Engineering. http://dms.library.utm.my:8080/vital/access/manager/Repository/vital:75130?queryType=vitalDismax&query=Structural+analysis+and+modeling+comparison+of+primates+dystrophin&public=true
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
language English
topic Unspecified
spellingShingle Unspecified
Mohajer, Faeze Sadat
Structural analysis and modeling comparison of primates dystrophin
description Dystrophin is a rod-shaped cytoplasmic protein which is an essential piece ofa protein complex that binds the cytoskeleton of a muscle fiber to the nearby extracellular matrix within the cell membrane. Lack of this protein in the muscle leads muscular dystrophy. Currently, Dystrophin structure has just been detected in human being. In fact, it has not been recognized in other types of primates. However, bioinformatics’ software has presented a big opportunity to predict its structure in other species on based on its structure in human being. The data for this project will be sourced by both bioinformatics databases and experimental information. The used databases were NCBI, PDB (protein data bank), UniProt, and Gene bank. The data that is gathered from these databases were analyzed using multiple sequence analysis software such as BLAST, Jalview to find conserved regions in the protein among the species of interest (different kinds of primates). In addition, the tertiary structure of the protein will be predicted by Swiss-model and will be observed and compared by 3-d structure viewing software such as: VMD and DeepView. In conclusion, the analysis of this study illustrates that Dystrophin has been changed slightly through evolution. However, the small changes that have been occurred have not affected the 3D structure and function of the protein.
format Thesis
author Mohajer, Faeze Sadat
author_facet Mohajer, Faeze Sadat
author_sort Mohajer, Faeze Sadat
title Structural analysis and modeling comparison of primates dystrophin
title_short Structural analysis and modeling comparison of primates dystrophin
title_full Structural analysis and modeling comparison of primates dystrophin
title_fullStr Structural analysis and modeling comparison of primates dystrophin
title_full_unstemmed Structural analysis and modeling comparison of primates dystrophin
title_sort structural analysis and modeling comparison of primates dystrophin
publishDate 2013
url http://eprints.utm.my/id/eprint/33293/1/FaezeSadatMohajerMFBME2013.pdf
http://eprints.utm.my/id/eprint/33293/
http://dms.library.utm.my:8080/vital/access/manager/Repository/vital:75130?queryType=vitalDismax&query=Structural+analysis+and+modeling+comparison+of+primates+dystrophin&public=true
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