ArticleJournal of molecular modeling2013
Molecular dynamics simulation of temperature induced unfolding of animal prion protein.
Article in Journal of molecular modeling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Ethanol Regulates Bitterness Perception of the Trp-Ile-Lys-Lys (WIKK) Peptide by Activating the Human Bitter Receptor T2R47.Foods (Basel, Switzerland) · 2026Article
- The Impact of Temperature and Pressure on the Structural Stability of Solvated Solid-State Conformations ofMaterials (Basel, Switzerland) · 2024Article
- Effects of the Temperature and Salt Concentration on the Structural Characteristics of the Protein (PDB Code 1BBL).Polymers · 2022Article
- Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg-white lysozyme.Veterinary medicine and science · 2021Article
- 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
- The role of Cys179-Cys214 disulfide bond in the stability and folding of prion protein: insights from molecular dynamics simulations.Journal of molecular modeling · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To elucidate the structural stability and the unfolding dynamics of the animal prion protein, the temperature induced structural evolution of turtle prion protein (tPrPc) and bank vole prion protein (bvPrPc) have been performed with molecular dynamics (MD) simulation. The unfolding behaviors of secondary structures showed that the α-helix was more stable than β-sheet. Extension and disruption of β-sheet commonly appeared in the temperature induced unfolding process. The conversion of α-helix to π-helix occurred more readily at the elevating temperature. Furthermore, it was suggested in this work that the unfolding of prion protein could be regulated by the temperature.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.