Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871197 | FEBS Letters | 2013 | 7 Pages |
Abstract
Various structural models for amyloid β fibrils have been derived from a variety of experimental techniques. However, these models cannot differentiate between the relative position of the two arms of the β hairpin called the stagger. Amyloid fibrils of various hierarchical levels form left-handed helices composed of β sheets. However it is unclear if positive, negative and zero staggers all form the macroscopic left-handed helices. To address this issue we have conducted extensive molecular dynamics simulations of amyloid β sheets of various staggers and shown that only negative staggers lead to the experimentally observed left-handed helices while positive staggers generate the incorrect right-handed helices. This result suggests that the negative staggers are physiologically relevant structure of the amyloid β fibrils.
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Authors
Pavan K. GhattyVenkataKrishna, Edward C. Uberbacher, Xiaolin Cheng,