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Hannah Baughman, Ph.D.

Assistant Professor of Biochemistry
Phone Number
Campus Mailbox



University of Washington
Cornell University

Current Research

Dr. Baughman investigates the role of protein dynamics in molecular function. She is particularly interested in intrinsically disordered proteins, which don't fold into a stable 3-dimensional structure but instead remain flexible in solution. Her research focuses on the involvement of intrinsically disordered proteins in the regulation of transcription.



Dr. Baughman teaches courses in biochemistry and biomedical sciences, including the following:
-TCHEM 405: Biochemistry I
-TCHEM 406: Biochemistry II
-TBIOMD 310: Foundational Skills in Biomedical Sciences
-TBIOMD 492: Critical Reading in Biomedical Sciences Literature
-TBIOMD 495: Biomedical Research Experience

Selected Publications

Baughman, H. E. R., Narang, D., Chen, W., Villagrán Suárez, A. C., Lee, J., Bachochin, M. J., Gunther, T. R., Wolynes, P. G., & Komives, E. A. (2022). An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFΚB p50/RELA. Journal of Biological Chemistry, 298(9), 102349.

Stormberg, T., Filliaux, S., Baughman, H. E. R., Komives, E. A., & Lyubchenko, Y. L. (2021). Transcription factor NF-ΚB unravels nucleosomes. Biochimica et Biophysica Acta (BBA) - General Subjects, 1865(9), 129934.

Baughman, H. E. R., Pham, T.-H. T., Adams, C. S., Nath, A., & Klevit, R. E. (2020). Release of a disordered domain enhances HSPB1 chaperone activity toward tau. Proceedings of the National Academy of Sciences, 117(6), 2923–2929.

Clouser, A. F., Baughman, H. E. R., Basanta, B., Guttman, M., Nath, A., & Klevit, R. E. (2019). Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of ‘quasi-ordered’ states. eLife, 8.

Baughman, H. E. R., Clouser, A. F., Klevit, R. E., & Nath, A. (2018). HSPB1 and HSC70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation. Journal of Biological Chemistry, 293(8), 2687–2700.