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Deep UV resonance Raman spectroscopy of ?-sheet amyloid fibrils: a QM/MM simulation.

ABSTRACT: We present a combined quantum mechanics and molecular mechanics study of the deep ultraviolet ??* resonance Raman spectra of ?-sheet amyloid fibrils A?(34-42) and A?(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(?)-H bending and N-D bending modes, rather than by peptide bond hydration.

SUBMITTER: Ren H

PROVIDER: S-EPMC3233492 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

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Deep UV resonance Raman spectroscopy of β-sheet amyloid fibrils: a QM/MM simulation.

Ren Hao H Jiang Jun J Mukamel Shaul S

The journal of physical chemistry. B 20111107 47

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 an ...[more]

PMID: 22007849

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