Deep UV resonance Raman spectroscopy of β-sheet amyloid fibrils: a QM/MM simulation.
We present a combined quantum mechanics and molecular mechanics study of the deep ultraviolet ππ* resonance Raman spectra of β-sheet amyloid fibrils Aβ(34-42) and Aβ(1-40). Effects of conformational fluctuations are described using a Ramachandran angle map, thus avoiding repeated ab initio calculations. Experimentally observed effects of hydrogen-deuterium exchange are reproduced. We propose that the AmIII band redshift upon deuteration is caused by the loss of coupling between C(α)-H bending and N-D bending modes, rather than by peptide bond hydration.
Department of Chemistry, University of California, Irvine, Irvine, California 92697, USA. haor@uci.edu
Hao
H
Ren
Jun
J
Jiang
Shaul
S
Mukamel
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D041961:Deuterium Exchange Measurement; D056004:Molecular Dynamics Simulation; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011789:Quantum Theory; D013059:Spectrum Analysis, Raman
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); C551682:amyloid beta-protein (34-42)