NMR assignments of human linker histone H1x N-terminal domain and globular domain in the presence and absence of perchlorate.
Biomol NMR Assign
; 13(1): 249-254, 2019 04.
Article
em En
| MEDLINE
| ID: mdl-30868366
ABSTRACT
Human linker histone H1 plays a seminal role in eukaryotic DNA packaging. H1 has a tripartite structure consisting of a central, conserved globular domain, which adopts a winged-helix fold, flanked by two variable N- and C-terminal domains. Here we present the backbone resonance assignments of the N-terminal domain and globular domain of human linker histone H1x in the presence and absence of the secondary structure stabilizer sodium perchlorate. Analysis of chemical shift changes between the two conditions is consistent with induction of transient secondary structural elements in the N-terminal domain of H1x in high ionic strength, which suggests that the N-terminal domain adopts significant alpha-helical conformations in the presence of DNA.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Histonas
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Compostos de Sódio
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Percloratos
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Ressonância Magnética Nuclear Biomolecular
Limite:
Humans
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article