ArticleBiophysical journal2007
Structural and hydration properties of the partially unfolded states of the prion protein.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Structural and cellular properties of human prion protein oligomers.Communications biology · 2025Article
- Effects of the Temperature and Salt Concentration on the Structural Characteristics of the Protein (PDB Code 1BBL).Polymers · 2022Article
- Dynamics of Amyloid Formation from Simplified Representation to Atomistic Simulations.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Mechanism of misfolding of the human prion protein revealed by a pathological mutation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Effect of Octapeptide Repeats on Prion Folding and Misfolding.International journal of molecular sciences · 2021Article
- Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein.Scientific reports · 2019Article
- Effects of pH and aggregation in the human prion conversion into scrapie form: a study using molecular dynamics with excited normal modes.European biophysics journal : EBJ · 2018Article
- Review
- Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.The Journal of biological chemistry · 2015Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- The intrinsic helical propensities of the helical fragments in prion protein under neutral and low pH conditions: a replica exchange molecular dynamics study.Journal of molecular modeling · 2013Article
- Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular Dynamics.Journal of chemical theory and computation · 2013Article
- Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition.Biochemistry · 2013Article
- Direct observation of multiple misfolding pathways in a single prion protein molecule.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Flexibility and binding affinity in protein-ligand, protein-protein and multi-component protein interactions: limitations of current computational approaches.Journal of the Royal Society, Interface · 2012Review
- Energy landscape of the prion protein helix 1 probed by metadynamics and NMR.Biophysical journal · 2012Article
- Modeling amyloid-beta as homogeneous dodecamers and in complex with cellular prion protein.PloS one · 2012Article
- Intrinsic determinants of Aβ(12-24) pH-dependent self-assembly revealed by combined computational and experimental studies.PloS one · 2011Article
- Influence of pH on the human prion protein: insights into the early steps of misfolding.Biophysical journal · 2010Article
- Highly polar environments catalyze the unfolding of PrP C helix 1.European biophysics journal : EBJ · 2010Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Misfolding and aggregation of the prion protein (PrP) is responsible for the development of transmissible spongiform encephalopathies (TSE). To gain insights into possible aggregation-prone intermediate states, we construct the free energy surface of the C-terminal globular domain of the PrP from enhanced sampling of replica exchange molecular dynamics. This cellular domain is characterized by three helices H1-H3 and a small beta-sheet. In agreement with experimental studies, the partially unfolded states display a stable core built from the central portions of helices H2 and H3 and a high mobility of helix H1 from the core. Among all identified conformational basins, a marginally populated state appears to be a very good candidate for aggregation. This intermediate is stabilized by four TSE-sensitive key interactions, displays a longer helix H1 with both a dry and solvated surface, and is featured by a significant detachment of helix H1 from the PrP-core.
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