title: Frequency distribution of the amide-I vibration sorted by residues in amyloid fibrils revealed by 2D-IR measurements and simulations.
abstract: The infrared optical response of amyloid fibrils Aβ(1-40) is investigated. Simulations of two models corresponding to different protonation states are compared with experiment. The simulations reveal that vibrational frequency distributions inside the fibrils are dominated by side chain fluctuations. We further confirm earlier suggestions based on 2D-IR measurements that water molecules can be trapped inside the fibrils.
authors.affiliation: Institut des Sciences Moléculaires d'Orsay, UMR CNRS 8214, Université Paris-Sud 11, 91405 Orsay, France. cyril.falvo@u-psud.fr
authors.forename: Cyril
authors.initials: C
authors.lastname: Falvo
authors.forename: Wei
authors.initials: W
authors.lastname: Zhuang
authors.forename: Yung Sam
authors.initials: YS
authors.lastname: Kim
authors.forename: Paul H
authors.initials: PH
authors.lastname: Axelsen
authors.forename: Robin M
authors.initials: RM
authors.lastname: Hochstrasser
authors.forename: Shaul
authors.initials: S
authors.lastname: Mukamel
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D010446:Peptide Fragments / Q000737:chemistry*; D013055:Spectrophotometry, Infrared; D014732:Vibration; D014867:Water / Q000737:chemistry
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); D014867:Water