Unravelling prion diseases using molecular dynamics simulations
Human prion diseases such as Creutzfeldt-Jakob disease are neurodegenerative diseases and present as infectious, sporadic and genetic disorders. Association of bovine spongiform encephalopathy (BSE) or 'mad cow disease' with human variant Creutzfeldt - Jakob disease (vCJD) have increased t...
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| Main Authors: | , , |
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| Format: | Book Section |
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Institute of Electrical and Electronics Engineers
2008
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| Subjects: | |
| Online Access: | http://eprints.utm.my/12791/ http://eprints.utm.my/12791/ http://eprints.utm.my/12791/ |
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| Summary: | Human prion diseases such as Creutzfeldt-Jakob disease are neurodegenerative diseases and present as infectious, sporadic and genetic disorders. Association of bovine spongiform encephalopathy (BSE) or 'mad cow disease' with human variant Creutzfeldt - Jakob disease (vCJD) have increased the attention on these diseases. Here we review and summarizes the use of molecular dynamics simulation to investigate the possible conformational transformation pathways of the prion protein (PrP) from its normal isoforms (PrPc) to a diseased scrapie isoforms (PrPsc). The review showed that although molecular dynamics simulations have been used in a variety of ways using various conditions such as pH, temperatures with diverse starting structures, the results showed consensus only on the creation of ß-sheets within the flexible N terminal, which is one possible characteristic of the PrPC to PrPC conversion. There is also a trend showing a research refocus from the flexible N terminal segment to the C terminal globular domain especially on second a-helix (H2), a segment linked to a cluster of point mutations. |
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