Structure, dynamics, and stability of the globular domain of human linker histone <scp>H1</scp> .0 and the role of positive charges-Reference-Cited by-同舟云学术

Structure, dynamics, and stability of the globular domain of human linker histone H1 .0 and the role of positive charges

Published:2022-02-23 Issue:4 Volume:31 Page:918-932
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Martinsen Jacob H.¹^ORCID,Saar Daniel¹^ORCID,Fernandes Catarina B.¹^ORCID,Schuler Benjamin²³^ORCID,Bugge Katrine¹^ORCID,Kragelund Birthe B.¹^ORCID

Affiliation:

1. REPIN and the Structural Biology and NMR Laboratory, The Linderstrøm‐Lang Centre for Protein Science, Department of Biology University of Copenhagen Copenhagen Denmark

2. Department of Biochemistry University of Zurich Zurich Switzerland

3. Department of Physics University of Zurich Zurich Switzerland

Funder

Novo Nordisk Fonden

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4281

Reference62 articles.

1. IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions—Insights from transcription factors

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3. Emerging roles of linker histones in regulating chromatin structure and function

4. Unspinning chromatin: Revealing the dynamic nucleosome landscape by NMR

5. A brief review of nucleosome structure

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