The Yin and Yang of protein folding
The study of protein aggregation saw a renaissance in the last decade, when it was discovered that aggregation is the cause of several human diseases, making this field of research one of the most exciting frontiers in science today. Building on knowledge about protein folding energy landscapes, det...
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| Veröffentlicht in: | The FEBS journal 2005-12, Vol.272 (23), p.5962-5970 |
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| container_end_page | 5970 |
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| container_title | The FEBS journal |
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| creator | Jahn, Thomas R. Radford, Sheena E. |
| description | The study of protein aggregation saw a renaissance in the last decade, when it was discovered that aggregation is the cause of several human diseases, making this field of research one of the most exciting frontiers in science today. Building on knowledge about protein folding energy landscapes, determined using an array of biophysical methods, theory and simulation, new light is now being shed on some of the key questions in protein‐misfolding diseases. This review will focus on the mechanisms of protein folding and amyloid fibril formation, concentrating on the role of partially folded states in these processes, the complexity of the free energy landscape, and the potentials for the development of future therapeutic strategies based on a full biophysical description of the combined folding and aggregation free‐energy surface. |
| doi_str_mv | 10.1111/j.1742-4658.2005.05021.x |
| format | Article |
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| ispartof | The FEBS journal, 2005-12, Vol.272 (23), p.5962-5970 |
| issn | 1742-464X 1742-4658 |
| language | eng |
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| source | Wiley Free Content; MEDLINE; IngentaConnect Free/Open Access Journals; Wiley Online Library Journals Frontfile Complete; Free Full-Text Journals in Chemistry |
| subjects | amyloid fibril formation Amyloidosis - metabolism Amyloidosis - physiopathology energy landscapes Energy Metabolism Humans intermediates misfolding Protein Conformation Protein Folding |
| title | The Yin and Yang of protein folding |
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