2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.

@article{Wang20112DIRSO,
  title={2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.},
  author={Lu Wang and Chris T. Middleton and Sadanand Singh and Allam S Reddy and Ann Marie Woys and David B Strasfeld and Peter J Marek and Daniel P Raleigh and Juan J de Pablo and Martin T Zanni and James L. Skinner},
  journal={Journal of the American Chemical Society},
  year={2011},
  volume={133 40},
  pages={16062-71}
}
The aggregation of human amylin to form amyloid contributes to islet β-cell dysfunction in type 2 diabetes. Studies of amyloid formation have been hindered by the low structural resolution or relatively modest time resolution of standard methods. Two-dimensional infrared (2DIR) spectroscopy, with its sensitivity to protein secondary structures and its intrinsic fast time resolution, is capable of capturing structural changes during the aggregation process. Moreover, isotope labeling enables the… CONTINUE READING
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