title: Effects of different force fields and temperatures on the structural character of Abeta (12-28) peptide in aqueous solution.
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.
authors.affiliation: Shandong Provincial Key Laboratory of Functional Macromolecular Biophysics, Dezhou University, 566 University Rd. West, Dezhou 253023, China; E-Mails:  qiayilai@mail.ustc.edu.cn  (Z.C.);  leiliusid@gmail.com  (L.L.);  zhaoll@sina.com  (L.Z.).
authors.forename: Zanxia
authors.initials: Z
authors.lastname: Cao
authors.forename: Lei
authors.initials: L
authors.lastname: Liu
authors.forename: Liling
authors.initials: L
authors.lastname: Zhao
authors.forename: Jihua
authors.initials: J
authors.lastname: Wang
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013696:Temperature
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C092395:amyloid beta-protein (12-28)