Computational, biochemical, and NMR-driven structural studies on histone variant H2A.B

Zhang, H.

Persistent URL of this record https://hdl.handle.net/1887/135944

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Zhang, H. (2020)

Computational, biochemical, and NMR-driven structural studies on histone variant H2A.B

Doctoral Thesis

Nature uses a special class of histone proteins, histone variants, to modulate the properties of chromatin at defined genomic locations. H2A.B is one of the most divergent H2A variants and is involved in important cellular functions, such as transcription and mRNA splicing. Incorporation of H2A.B in nucleosomes causes unwrapping of ~15 bp entry/ exit nucleosomal DNA from the histone octamer core. Yet, the molecular basis of such peculiar nucleosome conformation is unclear. The work described in this thesis aimed to determine the impact of H2A.B incorporation on the structural and dynamical properties of the nucleosome, primarily using nuclear magnetic resonance (NMR) spectroscopy.