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Apr 1, 2023 · As the most important protein–DNA complex, its structural and dynamic features have been successively revealed in recent years. However, its ...
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We define the bonding and specificity of divalent cation interaction with nucleosomal DNA by characterizing Mn2+ binding in the x-ray structure of the ...
Sep 4, 2022 · Here we report the cryo-electron microscopy structures of the p53 DNA-binding domain and the full-length p53 protein complexed with a nucleosome ...
The three-dimensional structure of the nucleosome core of chromatin showing the histone proteins and DNA in atomic detail is presented. 3. G Arents, EN ...
Nucleosome|Divalent Metal|Cation Binding|Counterion|Compaction|Chromosomal Protein|Dna-Binding|Methylation|Nucleosome Core|Nucleus|Structural Protein-Dna Complex from www.nature.com
Aug 29, 2022 · The MuvB core complex consists of a main scaffolding subunit called LIN9, the histone-binding protein RbBP4, the DNA-binding protein LIN54, and ...
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In this work, we studied the binding affinity and specificity for a series of TALE proteins under a variety of solution conditions using in vitro fluorescence ...
May 8, 2013 · Our study underscores this notion with a NMR analysis of the PWWP-nucleosome complex, a structural model of the complex based on experimental ...
Nucleosome|Divalent Metal|Cation Binding|Counterion|Compaction|Chromosomal Protein|Dna-Binding|Methylation|Nucleosome Core|Nucleus|Structural Protein-Dna Complex from www.sciencedirect.com
In eukaryotic cells, DNA interacts with two main types of binding proteins: transcription factors and histones. Histones form the core of nucleosomes and ...
Nucleosome|Divalent Metal|Cation Binding|Counterion|Compaction|Chromosomal Protein|Dna-Binding|Methylation|Nucleosome Core|Nucleus|Structural Protein-Dna Complex from pubs.rsc.org
Apr 6, 2016 · ... ions stabilize the protein structure and the enzyme–substrate complex. Introduction. A common type of DNA damage is an apurinic/apyrimidinic ...
Here we describe 11 crystal structures of nucleosome core particles containing individual point mutations in the structured regions of histones H3 and H4.