{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Reddy G"],"funding":["NIGMS NIH HHS"],"pagination":["1162-72"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3098509"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["113(4)"],"pubmed_abstract":["Recent experiments have shown that the congener Abeta(1-40)[D23-K28], in which the side chains of charged residues Asp23 and Lys28 are linked by a lactam bridge, forms amyloid fibrils that are structurally similar to the wild type (WT) Abeta peptide, but at a rate that is nearly 1000 times faster. We used all atom molecular dynamics simulations in explicit water, and two force fields, of the WT dimer, a monomer with the lactam bridge (Abeta(10-35)-lactam[D23-K28]), and the monomer and dimers with harmonically constrained D23-K28 salt bridge (Abeta(10-35)[D23-K28]) to understand the origin of the enhanced fibril rate formation. The simulations show that the assembly competent fibril-like monomer (N*) structure, which is present among the conformations sampled by the isolated monomer, with s"],"journal":["The journal of physical chemistry. B"],"pubmed_title":["Influence of preformed Asp23-Lys28 salt bridge on the conformational fluctuations of monomers and dimers of Abeta peptides with implications for rates of fibril formation."],"pmcid":["PMC3098509"],"funding_grant_id":["R01GM076688-05","R01 GM076688","R01 GM076688-08"],"pubmed_authors":["Reddy G","Straub JE","Thirumalai D"],"additional_accession":[]},"is_claimable":false,"name":"Influence of preformed Asp23-Lys28 salt bridge on the conformational fluctuations of monomers and dimers of Abeta peptides with implications for rates of fibril formation.","description":"Recent experiments have shown that the congener Abeta(1-40)[D23-K28], in which the side chains of charged residues Asp23 and Lys28 are linked by a lactam bridge, forms amyloid fibrils that are structurally similar to the wild type (WT) Abeta peptide, but at a rate that is nearly 1000 times faster. We used all atom molecular dynamics simulations in explicit water, and two force fields, of the WT dimer, a monomer with the lactam bridge (Abeta(10-35)-lactam[D23-K28]), and the monomer and dimers with harmonically constrained D23-K28 salt bridge (Abeta(10-35)[D23-K28]) to understand the origin of the enhanced fibril rate formation. The simulations show that the assembly competent fibril-like monomer (N*) structure, which is present among the conformations sampled by the isolated monomer, with s","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Jan","modification":"2025-04-19T16:29:46.682Z","creation":"2019-03-27T00:41:48Z"},"accession":"S-EPMC3098509","cross_references":{"pubmed":["19125574"],"doi":["10.1021/jp808914c"]}}