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Frontispiece: Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry
Proteins In their Communication on page 2340 ff., V. Forge, R. Antoine, and co‐workers report on the use of charge‐detection mass spectrometry for the characterization of amyloid fibrils. This method can be used to monitor protein aggregation in real time.
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Published in: | Angewandte Chemie International Edition 2016-02, Vol.55 (7), p.np-n/a |
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container_title | Angewandte Chemie International Edition |
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creator | Doussineau, Tristan Mathevon, Carole Altamura, Lucie Vendrely, Charlotte Dugourd, Philippe Forge, Vincent Antoine, Rodolphe |
description | Proteins In their Communication on page 2340 ff., V. Forge, R. Antoine, and co‐workers report on the use of charge‐detection mass spectrometry for the characterization of amyloid fibrils. This method can be used to monitor protein aggregation in real time. |
doi_str_mv | 10.1002/anie.201680761 |
format | article |
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subjects | Agglomeration amyloids Fibrils Mass spectrometry Mass spectroscopy Protein interaction Proteins Real time Scientific imaging self-assembly Water analysis Workers β-Amyloid |
title | Frontispiece: Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry |
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