Fast Motions of Key Methyl Groups in Amyloid-β Fibrils

• Published in: Biophysical journal Vol. 111; no. 10; pp. 2135 - 2148
• Main Authors: Vugmeyster, Liliya, Ostrovsky, Dmitry, Clark, Matthew A., Falconer, Isaac B., Hoatson, Gina L., Qiang, Wei
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.11.2016; Elsevier; The Biophysical Society
• Subjects: Amino Acid Sequence; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - genetics; Amyloid beta-Peptides - metabolism; Hydrophobic and Hydrophilic Interactions; Kinetics; Movement; Mutation; Peptide Fragments - chemistry; Peptide Fragments - genetics; Peptide Fragments - metabolism; Protein Multimerization; Protein Structure, Secondary; Proteins

Amyloid-β (Aβ) peptide is the major component of plaques found in Alzheimer’s disease patients. Using solid-state 2H NMR relaxation performed on selectively deuterated methyl groups, we probed the dynamics in the threefold symmetric and twofold symmetric polymorphs of native Aβ as well as the protof...