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Molecular dynamic simulation of V176G mutation associated with Gerstmann–Sträussler–Scheinker at elevated temperature

The transformation of cellular prion protein (PrPc) into pathogenic conformer (PrPSc) in transmissible spongiform encephalopathy is expedited by mutations in the prion protein. One recently reported novel mutation V176G is located in region of the protein known to cause Creutzfeldt-Jakob disease (CJ...

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Main Authors: Jomah, A. F., Shamsir, M. S.
Format: Article
Language:English
Published: Penerbit UTM Press 2016
Subjects:
SB Plant culture
Online Access:http://eprints.utm.my/id/eprint/70013/1/AshrafFadilJomah2016_MolecularDynamicSimulationOfV176GMutation.pdf
http://eprints.utm.my/id/eprint/70013/
http://dx.doi.org/10.11113/jt.v78.5200
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spelling my.utm.700132017-11-14T06:23:14Z http://eprints.utm.my/id/eprint/70013/ Molecular dynamic simulation of V176G mutation associated with Gerstmann–Sträussler–Scheinker at elevated temperature Jomah, A. F. Shamsir, M. S. SB Plant culture The transformation of cellular prion protein (PrPc) into pathogenic conformer (PrPSc) in transmissible spongiform encephalopathy is expedited by mutations in the prion protein. One recently reported novel mutation V176G is located in region of the protein known to cause Creutzfeldt-Jakob disease (CJD) but possess a unique neuropathological profile and spongiform alteration similar to Gerstmann–Sträussler–Scheinker syndrome (GSS). Using molecular dynamics simulations; the denaturation of the prion structure with V176G at 500K was studied to identify the dynamics in structural properties such as salt bridge, solvent accessibility, hydrogen bonds and hydrophobicity. The simulations revealed that the heat-induced unfolding caused destabilization of the native structure of PrP and affecting the ß-sheet region of the structure more than the a-helix. Unique salt bridge formation suggests conformational orientation that may be attributed to the V176G mutation. The mutation effects showed an increased fluctuation of the H1 region, gain of hydrogen bonds between H3 and H2 which may be part of the oligomerization pathway and determine the features of the PrPSc assemblies. Penerbit UTM Press 2016 Article PeerReviewed application/pdf en http://eprints.utm.my/id/eprint/70013/1/AshrafFadilJomah2016_MolecularDynamicSimulationOfV176GMutation.pdf Jomah, A. F. and Shamsir, M. S. (2016) Molecular dynamic simulation of V176G mutation associated with Gerstmann–Sträussler–Scheinker at elevated temperature. Jurnal Teknologi, 78 (2). pp. 99-105. ISSN 0127-9696 http://dx.doi.org/10.11113/jt.v78.5200 DOI:10.11113/jt.v78.5200
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 SB Plant culture
spellingShingle SB Plant culture
Jomah, A. F.
Shamsir, M. S.
Molecular dynamic simulation of V176G mutation associated with Gerstmann–Sträussler–Scheinker at elevated temperature
description The transformation of cellular prion protein (PrPc) into pathogenic conformer (PrPSc) in transmissible spongiform encephalopathy is expedited by mutations in the prion protein. One recently reported novel mutation V176G is located in region of the protein known to cause Creutzfeldt-Jakob disease (CJD) but possess a unique neuropathological profile and spongiform alteration similar to Gerstmann–Sträussler–Scheinker syndrome (GSS). Using molecular dynamics simulations; the denaturation of the prion structure with V176G at 500K was studied to identify the dynamics in structural properties such as salt bridge, solvent accessibility, hydrogen bonds and hydrophobicity. The simulations revealed that the heat-induced unfolding caused destabilization of the native structure of PrP and affecting the ß-sheet region of the structure more than the a-helix. Unique salt bridge formation suggests conformational orientation that may be attributed to the V176G mutation. The mutation effects showed an increased fluctuation of the H1 region, gain of hydrogen bonds between H3 and H2 which may be part of the oligomerization pathway and determine the features of the PrPSc assemblies.
format Article
author Jomah, A. F.
Shamsir, M. S.
author_facet Jomah, A. F.
Shamsir, M. S.
author_sort Jomah, A. F.
title Molecular dynamic simulation of V176G mutation associated with Gerstmann–Sträussler–Scheinker at elevated temperature
title_short Molecular dynamic simulation of V176G mutation associated with Gerstmann–Sträussler–Scheinker at elevated temperature
title_full Molecular dynamic simulation of V176G mutation associated with Gerstmann–Sträussler–Scheinker at elevated temperature
title_fullStr Molecular dynamic simulation of V176G mutation associated with Gerstmann–Sträussler–Scheinker at elevated temperature
title_full_unstemmed Molecular dynamic simulation of V176G mutation associated with Gerstmann–Sträussler–Scheinker at elevated temperature
title_sort molecular dynamic simulation of v176g mutation associated with gerstmann–sträussler–scheinker at elevated temperature
publisher Penerbit UTM Press
publishDate 2016
url http://eprints.utm.my/id/eprint/70013/1/AshrafFadilJomah2016_MolecularDynamicSimulationOfV176GMutation.pdf
http://eprints.utm.my/id/eprint/70013/
http://dx.doi.org/10.11113/jt.v78.5200
_version_ 1643656072767995904
score 13.211869

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