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Deuteron Solid-state NMR Relaxation Measurements Reveal Two Distinct Conformational Exchange Processes in the Disordered N-terminal Domain of Amyloid-β Fibrils

We employed deuterium solid-state NMR techniques under static conditions to discern the details of the μs-ms timescale motions in the flexible N-terminal subdomain of Aβ(1-40) amyloid fibrils, which spans residues 1–16. In particular, we utilized a rotating frame (R(1ρ)) and the newly developed time...

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Detalhes bibliográficos
Publicado no:Chemphyschem
Main Authors: Vugmeyster, Liliya, Au, Dan Fai, Ostrovsky, Dmitry, Fu, Riqiang
Formato: Artigo
Idioma:Inglês
Publicado em: 2019
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC6663588/
https://ncbi.nlm.nih.gov/pubmed/31087613
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/cphc.201900363
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