Structural diversity and initial oligomerization of PrP106-126 studied by replica-exchange and conventional molecular dynamics simulations.

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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Bibliographic Details
Main Authors: Lulu Ning, Jingjing Guo, Qifeng Bai, Nengzhi Jin, Huanxiang Liu, Xiaojun Yao
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24586266/pdf/?tool=EBI

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https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24586266/pdf/?tool=EBI

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