Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.

@article{Melckebeke2011ProbingWA,
  title={Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.},
  author={H{\'e}l{\`e}ne Van Melckebeke and Paul Schanda and Julia Gath and Christian Wasmer and Ren{\'e} Verel and Adam Lange and Beat H Meier and Anja B{\"o}ckmann},
  journal={Journal of molecular biology},
  year={2011},
  volume={405 3},
  pages={
          765-72
        }
}
Despite the importance of protein fibrils in the context of conformational diseases, information on their structure is still sparse. Hydrogen/deuterium exchange measurements of backbone amide protons allow the identification hydrogen-bonding patterns and reveal pertinent information on the amyloid β-sheet architecture. However, they provide only little information on the identity of residues exposed to solvent or buried inside the fibril core. NMR spectroscopy is a potent method for identifying… CONTINUE READING
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