Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide
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....
Main Authors: | Liu, Lei, Li, Qiang, Zhang, Shuai, Wang, Xiaofeng, Hoffmann, Søren Vrønning, Li, Jingyuan, Liu, Zheng, Besenbacher, Flemming, Dong, Mingdong |
---|---|
Other Authors: | School of Materials Science & Engineering |
Format: | Journal Article |
Language: | English |
Published: |
2017
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/85006 http://hdl.handle.net/10220/42054 |
Similar Items
-
Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates
by: Maho Yagi-Utsumi, et al.
Published: (2022-07-01) -
Gels of Amyloid Fibers
by: Ruizhi Wang, et al.
Published: (2019-05-01) -
Revealing the Nanoarchitectonics of Amyloid β‐Aggregation on Two‐Dimensional Biomimetic Membranes by Surface‐Enhanced Infrared Absorption Spectroscopy
by: Manyu Zhu, et al.
Published: (2023-02-01) -
Structural insight into Escherichia coli CsgA amyloid fibril assembly
by: Fan Bu, et al.
Published: (2024-04-01) -
Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42
by: Ruitian Liu, et al.
Published: (2005-10-01)