Hannah Baughman, Ph.D.
About
Degrees
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.
Teaching
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
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. https://doi.org/10.1016/j.jbc.2022.102349
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. https://doi.org/10.1016/j.bbagen.2021.129934
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. https://doi.org/10.1073/pnas.1915099117
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. https://doi.org/10.7554/elife.50259
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. https://doi.org/10.1074/jbc.m117.803411