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DC Field | Value | Language |
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dc.contributor.author | Tolchard, J. | - |
dc.contributor.author | Pandey, M.K. | - |
dc.contributor.author | Berbon, M. | - |
dc.contributor.author | Noubhan, A. | - |
dc.contributor.author | Saupe, S.J. | - |
dc.contributor.author | Nishiyama, Y. | - |
dc.contributor.author | Habenstein, B. | - |
dc.contributor.author | Loquet, A. | - |
dc.date.accessioned | 2019-01-01T07:16:59Z | - |
dc.date.available | 2019-01-01T07:16:59Z | - |
dc.date.issued | 2019-01-01 | - |
dc.identifier.uri | http://localhost:8080/xmlui/handle/123456789/1175 | - |
dc.description.abstract | We present a new solid-state NMR proton-detected three-dimensional experiment dedicated to the observation of protein proton side chain resonances in nano-liter volumes. The experiment takes advantage of very fast magic angle spinning and double quantum 13C–13C transfer to establish efficient (H)CCH correlations detected on side chain protons. Our approach is demonstrated on the HET-s prion domain in its functional amyloid fibrillar form, fully protonated, with a sample amount of less than 500 µg using a MAS frequency of 70 kHz. The majority of aliphatic and aromatic side chain protons (70%) are observable, in addition to Hα resonances, in a single experiment providing a complementary approach to the established proton-detected amide-based multidimensional solid-state NMR experiments for the study and resonance assignment of biosolid samples, in particular for aromatic side chain resonances. | en_US |
dc.language.iso | en_US | en_US |
dc.subject | Amyloid fibrils | en_US |
dc.subject | Solid-state NMR | en_US |
dc.subject | Proton detection | en_US |
dc.subject | Very fast MAS | en_US |
dc.subject | Protein NMR | en_US |
dc.title | Detection of side-chain proton resonances of fully protonated biosolids in nano-litre volumes by magic angle spinning solid-state NMR | en_US |
dc.type | Article | en_US |
Appears in Collections: | Year-2018 |
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Full Text.pdf | 1.37 MB | Adobe PDF | View/Open Request a copy |
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