Volume and energy folding landscape of prion protein revealed by pressure
The main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pre...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Associação Brasileira de Divulgação Científica
2005-08-01
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| Series: | Brazilian Journal of Medical and Biological Research |
| Subjects: | |
| Online Access: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800006 |
| _version_ | 1818421485416480768 |
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| author | Y. Cordeiro J. Kraineva R. Winter J.L. Silva |
| author_facet | Y. Cordeiro J. Kraineva R. Winter J.L. Silva |
| author_sort | Y. Cordeiro |
| collection | DOAJ |
| description | The main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pressure as a tool to investigate this structural transition and to populate possible intermediates in the folding/unfolding pathway of the prion protein. The latest findings on the application of high pressure to the cellular prion protein and to the scrapie PrP forms will be summarized in this review, which focuses on the energetic and volumetric properties of prion folding and conversion. |
| first_indexed | 2024-12-14T13:11:07Z |
| format | Article |
| id | doaj.art-bc1ec7edaf2247a3b74c71cfe4c00784 |
| institution | Directory Open Access Journal |
| issn | 0100-879X 1414-431X |
| language | English |
| last_indexed | 2024-12-14T13:11:07Z |
| publishDate | 2005-08-01 |
| publisher | Associação Brasileira de Divulgação Científica |
| record_format | Article |
| series | Brazilian Journal of Medical and Biological Research |
| spelling | doaj.art-bc1ec7edaf2247a3b74c71cfe4c007842022-12-21T23:00:12ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X2005-08-013881195120110.1590/S0100-879X2005000800006Volume and energy folding landscape of prion protein revealed by pressureY. CordeiroJ. KrainevaR. WinterJ.L. SilvaThe main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie). The formation of this abnormal isoform then triggers the transmissible spongiform encephalopathies. Here, we discuss the use of high pressure as a tool to investigate this structural transition and to populate possible intermediates in the folding/unfolding pathway of the prion protein. The latest findings on the application of high pressure to the cellular prion protein and to the scrapie PrP forms will be summarized in this review, which focuses on the energetic and volumetric properties of prion folding and conversion.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800006PrionHigh pressureStructural conversionAggregation |
| spellingShingle | Y. Cordeiro J. Kraineva R. Winter J.L. Silva Volume and energy folding landscape of prion protein revealed by pressure Brazilian Journal of Medical and Biological Research Prion High pressure Structural conversion Aggregation |
| title | Volume and energy folding landscape of prion protein revealed by pressure |
| title_full | Volume and energy folding landscape of prion protein revealed by pressure |
| title_fullStr | Volume and energy folding landscape of prion protein revealed by pressure |
| title_full_unstemmed | Volume and energy folding landscape of prion protein revealed by pressure |
| title_short | Volume and energy folding landscape of prion protein revealed by pressure |
| title_sort | volume and energy folding landscape of prion protein revealed by pressure |
| topic | Prion High pressure Structural conversion Aggregation |
| url | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800006 |
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