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Combined Solution‐ and Magic Angle Spinning NMR Reveals Regions of Distinct Dynamics in Amyloid β Protofibrils
Author(s) -
Lendel Christofer,
Sparrman Tobias,
Mayzel Maxim,
Andersson C. Evalena,
Karlsson Göran,
Härd Torleif
Publication year - 2016
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201601468
Subject(s) - magic angle spinning , amyloid (mycology) , solid state nuclear magnetic resonance , characterization (materials science) , molecular dynamics , amyloid fibril , chemistry , spinning , dynamics (music) , crystallography , materials science , nuclear magnetic resonance spectroscopy , biophysics , amyloid β , chemical physics , nuclear magnetic resonance , nanotechnology , physics , stereochemistry , computational chemistry , biology , polymer chemistry , medicine , inorganic chemistry , disease , pathology , acoustics
Solid‐state magic angle spinning (MAS) NMR has emerged as an important tool for investigations of protein aggregates and amyloid fibrils, which are not accessible for solution NMR experiments. We recently presented a structural model for amyloid β (Aβ) protofibrils based on MAS‐NMR data. The absence of resonances for the N‐terminus of Aβ in this dataset suggested that it might be disordered and more dynamic than the structural core. We here provide evidence for a distinct dynamic regime in the N‐terminal part of the peptide and show that the structural characteristics of this region can be elucidated using 13 C‐detected solution NMR. The results shed more light on the structural properties of pre‐fibrillar Aβ species and demonstrate the potential of combining MAS and solution NMR experiments for the characterization of structure and dynamics of complex protein assemblies.