Ontology highlight
ABSTRACT:
SUBMITTER: Liu L
PROVIDER: S-EPMC5071675 | biostudies-literature | 2016 Jun
REPOSITORIES: biostudies-literature
Liu Lei L Li Qiang Q Zhang Shuai S Wang Xiaofeng X Hoffmann Søren Vrønning SV Li Jingyuan J Liu Zheng Z Besenbacher Flemming F Dong Mingdong M
Advanced science (Weinheim, Baden-Wurttemberg, Germany) 20160408 6
The differentiation of protein properties and biological functions arises from the variation in the primary and secondary structure. Specifically, in abnormal assemblies of protein, such as amyloid peptide, the secondary structure is closely correlated with the stable ensemble and the cytotoxicity. In this work, the early Aβ<sub>33-42</sub> aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide Aβ<sub>33-42</sub> consistin ...[more]