Abstract
(Figure Presented) The structural basis for polymorphism in amyloids is unraveled with a model system. The hydrogen-bonding pattern within the β sheets of fibrils is strongly influenced by the pH of the solution from which the fibrils are formed. Solid-state NMR spectroscopy experiments allow quantification of the relative amounts of two different β-sheet structures over the pH range 2.0-7.3. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
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Verel, R., Tomka, I. T., Bertozzi, C., Cadalbert, R., Kammerer, R. A., Steinmetz, M. O., & Meier, B. H. (2008). Polymorphism in an amyloid-like fibril-forming model peptide. Angewandte Chemie - International Edition, 47(31), 5842–5845. https://doi.org/10.1002/anie.200800021
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