ArticleInternational journal of molecular sciences2011
Effects of different force fields and temperatures on the structural character of Abeta (12-28) peptide in aqueous solution.
Article in International journal of molecular sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- In Silico Discovery of Potential Inhibitors Targeting the RNA Binding Loop of ADAR2 and 5-HT2CR from Traditional Chinese Natural Compounds.International journal of molecular sciences · 2023Article
- Molecular Docking and Dynamics Simulation Studies Predict Potential Anti-ADAR2 Inhibitors: Implications for the Treatment of Cancer, Neurological, Immunological and Infectious Diseases.International journal of molecular sciences · 2023Article
- On the Conformational Dynamics of β-Amyloid Forming Peptides: A Computational Perspective.Frontiers in bioengineering and biotechnology · 2020Review
- Effects of All-Atom Molecular Mechanics Force Fields on Amyloid Peptide Assembly: The Case of AβJournal of chemical theory and computation · 2019Article
- Investigating Ebola virus pathogenicity using molecular dynamics.BMC genomics · 2017Article
- Conformational changes in amyloid-beta (12-28) alloforms studied using action-FRET, IMS and molecular dynamics simulations.Chemical science · 2015Article
- Temperature dependence of Congo red binding to amyloid β12-28.European biophysics journal : EBJ · 2013Article
- Comparison of the structural characteristics of Cu(2+)-bound and unbound α-syn12 peptide obtained in simulations using different force fields.Journal of molecular modeling · 2013Article
- The effect of C-terminal helix on the stability of FF domain studied by molecular dynamics simulation.International journal of molecular sciences · 2012Article
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Authors and funding
4 authors.
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Abstract
The aim of this work is to investigate the effects of different force fields and temperatures on the structural character of Aβ (12-28) peptide in aqueous solution. Moreover, the structural character of Aβ (12-28) peptide is compared with other amyloid peptides (such as H1 and α-syn12 peptide). The two independent temperature replica exchange molecular dynamics (T-REMD) simulations were completed by using two different models (OPLS-AA/TIP4P and GROMOS 43A1/SPC). We compared the models by analyzing the distributions of backbone dihedral angles, the secondary structure propensity, the free energy surface and the formation of β-hairpin. The results show that the mostly populated conformation state is random coil for both models. The population of β-hairpin is below 8 percent for both models. However, the peptide modeled by GROMOS 43A1 form β-hairpin with turn located at residues F19-E22, while the peptide modeled by OPLS-AA form β-hairpin with turn located at residues L17-F20.
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