Open AccessProtein Structures: Identification of a Novel Parallel β‐Strand Conformation within Molecular Monolayer of Amyloid Peptide (Adv. Sci. 6/2016)
Author(s) -
Liu Lei,
Li Qiang,
Zhang Shuai,
Wang Xiaofeng,
Hoffmann Søren Vrønning,
Li Jingyuan,
Liu Zheng,
Besenbacher Flemming,
Dong Mingdong
Publication year - 2016
Publication title -
advanced science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.388
H-Index - 100
ISSN - 2198-3844
DOI - 10.1002/advs.201670032
Subject(s) - amyloid (mycology) , peptide , monolayer , amyloid β , amyloid fibril , pathogenesis , identification (biology) , chemistry , biochemistry of alzheimer's disease , computational biology , disease , biophysics , biochemistry , amyloid precursor protein , medicine , alzheimer's disease , biology , pathology , inorganic chemistry , botany
Alzheimer's disease is the most common form of dementia, with amyloid protein assembly associated with the pathogenesis of disease. Thus it is of utmost importance to reveal the detailed structure of the amyloid protein aggregates. In article 1500369, F. Besenbacher, M. Dong and co‐workers discover a new parallel‐like β‐strand molecular monolayer structure of amyloid peptide at hydrophobic interfaces.