Dynamic domains of amyloid fibrils can be site-specifically assigned with proton detected 3D NMR spectroscopy.
J Biomol NMR
; 66(3): 159-162, 2016 11.
Article
em En
| MEDLINE
| ID: mdl-27766502
ABSTRACT
Several amyloid fibrils have cores framed by highly dynamic, intrinsically disordered, domains that can play important roles for function and toxicity. To study these domains in detail using solid-state NMR spectroscopy, site-specific resonance assignments are required. Although the rapid dynamics of these domains lead to considerable averaging of orientation-dependent NMR interactions and thereby line-narrowing, the proton linewidths observed in these samples is far larger than what is regularly observed in solution. Here, we show that it is nevertheless possible to record 3D HNCO, HNCA, and HNcoCA spectra on these intrinsically disordered domains and to obtain site-specific assignments.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Prótons
/
Espectroscopia de Ressonância Magnética
/
Domínios Proteicos
/
Amiloide
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article