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pro vyhledávání: '"Herna de Wit"'
Publikováno v:
Data in Brief, Vol 31, Iss , Pp 105865- (2020)
Linker histone H1 plays a vital role in the packaging of DNA. H1 has a tripartite structure: a conserved central globular domain that adopts a winged-helix fold, flanked by highly variable and intrinsically unstructured N- and C-terminal domains. The
Externí odkaz:
https://doaj.org/article/c9060691cbb9450d8a144bd1d458a5d7
Autor:
Herna de Wit, Gerrit Koorsen
Publikováno v:
Data in Brief, Vol 30, Iss , Pp 105580- (2020)
Human linker histones (H1s) are important in chromatin packaging and condensation. The central globular domain of H1 anchors the protein to the nucleosome. The nucleosomal binding modes of different H1 globular domains may affect nucleosomal DNA acce
Externí odkaz:
https://doaj.org/article/170dbc392cbf4020b041d83d9e18a8c4
Autor:
Gerrit Koorsen, Herna de Wit
Publikováno v:
Data in Brief
Data in Brief, Vol 30, Iss, Pp 105580-(2020)
Data in Brief, Vol 30, Iss, Pp 105580-(2020)
Human linker histones (H1s) are important in chromatin packaging and condensation. The central globular domain of H1 anchors the protein to the nucleosome. The nucleosomal binding modes of different H1 globular domains may affect nucleosomal DNA acce
Publikováno v:
Data in Brief
Data in Brief, Vol 31, Iss, Pp 105865-(2020)
Data in Brief, Vol 31, Iss, Pp 105865-(2020)
Linker histone H1 plays a vital role in the packaging of DNA. H1 has a tripartite structure: a conserved central globular domain that adopts a winged-helix fold, flanked by highly variable and intrinsically unstructured N- and C-terminal domains. The
Publikováno v:
Biomolecular NMR assignments. 13(1)
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 p