Impact of Deuteration on the Assembly Kinetics of Transthyretin Monitored by Native Mass Spectrometry and Implications for Amyloidoses
It is well established that the formation of transthyretin (TTR) amyloid fibrils is linked to the destabilization and dissociation of its tetrameric structure into insoluble aggregates. Isotope labeling is used for the study of TTR by NMR, neutron diffraction, and mass spectrometry (MS). Here MS, th...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
John Wiley and Sons Inc.
2016
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5094506/ |