Structural diversity and initial oligomerization of PrP106-126 studied by replica-exchange and conventional molecular dynamics simulations.
Prion diseases are marked by cerebral accumulation of the abnormal isoform of the prion protein. A fragment of prion protein composed of residues 106-126 (PrP106-126) exhibits similar properties to full length prion and plays a key role in the conformational conversion from cellular prion to its pat...
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| Auteurs principaux: | , , , , , |
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| Format: | article |
| Langue: | EN |
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Public Library of Science (PLoS)
2014
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| Accès en ligne: | https://doaj.org/article/65dcfc70056f434baecb14715d468476 |
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