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|National Institutes of Health, USA|
|ScientificTracks Abstracts: J Proteomics Bioinform|
|Human genome is packaged into chromatin through association with small positively charged histone proteins. The structural unit of chromatin is the nucleosome, which consists of ~147 bp of DNA and two copies of each of the four core histones (H2A, H2B, H3 and H4). Numerous proteins regulate chromatin structure and function through specific binding to the nucleosome. The structural basis of many of these interactions is unknown. Structural determination of the nucleosome in complex with a protein by X-ray crystallography and single particle cryo-EM has proven to be very challenging in many cases due to difficulties to crystalize them and dissociation of the complex during cryo-processes. On the other hand, the nucleosome is too large (>200 KDa) for structural studies with conventional NMR methods. We have used methyl-TROSY coupled with site-specific mutagenesis and paramagnetic spin labeling to investigate how the nucleosome is recognized by various chromatin factor proteins, including high-mobility group nucleosomal protein, centromere protein C and linker histones. Major results and future perspectives will be presented.|
Yawen Bai has received his PhD in Biophysics from the University of Pennsylvania Medical School. After Postdoctoral work at the Scripps Research Institute, La Jolla, California, he became an Investigator at the National Cancer Institute of the National Institutes of Health in Bethesda, Maryland since 1997. The research interests of his group include structural studies on protein folding intermediates, histone chaperones, epigenetic specification of centromeres and chromatin folding.
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