{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Miller Y"],"funding":["Intramural NIH HHS","NCI NIH HHS"],"pagination":["1168-77"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2726324"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["97(4)"],"pubmed_abstract":["Abeta(17-42) (so-called p3) amyloid is detected in vivo in the brains of individuals with Alzheimer's disease or Down's syndrome. We investigated the polymorphism of Abeta(17-42) oligomers based on experimental data from steady-state NMR measurements, electron microscopy, two-dimensional hydrogen exchange, and mutational studies, using all-atom molecular-dynamics simulation with explicit solvent. We assessed the structural stability and the populations. Our results suggest that conformational differences in the U-turn of Abeta(17-42) lead to polymorphism in beta-sheet registration and retention of an ordered beta-strand organization at the termini. Further, although the parallel Abeta(17-42) oligomer organization is the most stable of the conformers investigated here, different antiparalle"],"journal":["Biophysical journal"],"pubmed_title":["Polymorphism of Alzheimer's Abeta17-42 (p3) oligomers: the importance of the turn location and its conformation."],"pmcid":["PMC2726324"],"funding_grant_id":["N01-CO-12400","N01 CO012400"],"pubmed_authors":["Ma B","Miller Y","Nussinov R"],"additional_accession":[]},"is_claimable":false,"name":"Polymorphism of Alzheimer's Abeta17-42 (p3) oligomers: the importance of the turn location and its conformation.","description":"Abeta(17-42) (so-called p3) amyloid is detected in vivo in the brains of individuals with Alzheimer's disease or Down's syndrome. We investigated the polymorphism of Abeta(17-42) oligomers based on experimental data from steady-state NMR measurements, electron microscopy, two-dimensional hydrogen exchange, and mutational studies, using all-atom molecular-dynamics simulation with explicit solvent. We assessed the structural stability and the populations. Our results suggest that conformational differences in the U-turn of Abeta(17-42) lead to polymorphism in beta-sheet registration and retention of an ordered beta-strand organization at the termini. Further, although the parallel Abeta(17-42) oligomer organization is the most stable of the conformers investigated here, different antiparalle","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Aug","modification":"2026-05-02T23:05:51.049Z","creation":"2026-04-07T18:36:34.507Z"},"accession":"S-EPMC2726324","cross_references":{"pubmed":["19686665"],"doi":["10.1016/j.bpj.2009.05.042"]}}