Hanqiao Feng, Ph.D.

Staff Scientist
Laboratory of Biochemistry and Molecular Biology

Team Member of:

Yawen Bai, Ph.D.

Our studies are focused on the structural basis of how proteins like histone chaperone, liker histones, and chromatin remodelers bind to nucleosome, modulate chromatin structure, mediate the nuclear processes like DNA repair, gene transcription, and ensure accurate segregation of chromosome. We pioneered the structural determination of protein-protein complex and protein in the complex with nucleosome by high-resolution nuclear magnetic resonance (NMR) and X-ray crystallography.

Areas of Expertise
structural biology, biophysics, structural determination of protein-protein complex, protein-nucleosome complex, NMR, X-ray crystallography

Contact Info

Hanqiao Feng, Ph.D.
Center for Cancer Research
National Cancer Institute
Building 37, Room 6114
Bethesda, MD 20892-4260
Ph: 301-496-1581
fengh@mail.nih.gov
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Selected Publications

  1. Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3.
    Zhou Z, Feng H, Zhou BR, Ghirlando R, Hu K, Zwolak A, Miller Jenkins LM, Xiao H, Tjandra N, Wu C, Bai Y.
    Nature. 472: 234-7, 2011. [ Journal Article ]
  2. A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C.
    Kato H, Jiang J, Zhou BR, Rozendaal M, Feng H, Ghirlando R, Xiao TS, Straight AF, Bai Y.
    Science. 340: 1110-3, 2013. [ Journal Article ]
  3. Structural insights into the histone H1-nucleosome complex.
    Zhou BR, Feng H, Kato H, Dai L, Yang Y, Zhou Y, Bai Y.
    Proc. Natl. Acad. Sci. U.S.A.. 110: 19390-5, 2013. [ Journal Article ]
  4. The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer.
    Hong J, Feng H, Wang F, Ranjan A, Chen J, Jiang J, Ghirlando R, Xiao TS, Wu C, Bai Y.
    Mol. Cell. 53: 498-505, 2014. [ Journal Article ]
  5. NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B.
    Zhou Z, Feng H, Hansen DF, Kato H, Luk E, Freedberg DI, Kay LE, Wu C, Bai Y.
    Nat. Struct. Mol. Biol.. 15: 868-9, 2008. [ Journal Article ]