Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations.

@article{Wu2009StructuralRO,
  title={Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations.},
  author={Kuen-Phon Wu and Daniel S. Weinstock and Chitra Narayanan and Ronald M. Levy and J. M. Baum},
  journal={Journal of molecular biology},
  year={2009},
  volume={391 4},
  pages={
          784-96
        }
}
alpha-Synuclein is an intrinsically disordered protein that appears in aggregated forms in the brains of patients with Parkinson's disease. The conversion from monomer to aggregate is complex, and aggregation rates are sensitive to changes in amino acid sequence and environmental conditions. It has previously been observed that alpha-synuclein aggregates faster at low pH than at neutral pH. Here, we combine NMR spectroscopy and molecular simulations to characterize alpha-synuclein… CONTINUE READING
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