Research Collaborate Lab Bench

Emma Morrison, PhD

Assistant Professor


  • TBRC C2980

Contact Information

General Interests

Nucleosome structure, dynamics, and mechanisms of regulation using biophysical techniques including NMR spectroscopy.


Post-doctoral training, University of Iowa, 2014-2019
PhD, Washington University in St. Louis, 2014
BA, Johns Hopkins University, 2008


Dr. Morrison received her Bachelor of Arts in Chemistry from Johns Hopkins University. She continued on to study mechanisms of broad ligand specificity in a multi-drug resistance transporter (EmrE) with Dr. Katherine Henzler-Wildman, receiving her PhD in Molecular Biophysics from Washington University in St. Louis. From there, Dr. Morrison transitioned into the field of chromatin regulation as a postdoctoral fellow with Dr. Catherine Musselman at the University of Iowa. There, she became interested in nucleosome structure and dynamics. During her postdoctoral studies, she was awarded a fellowship from the Arnold and Mabel Beckman Foundation. Dr. Morrison joined the faculty at the Medical College of Wisconsin in 2019 where she continues her investigation into the role of histone tail conformation and dynamics in chromatin regulation.

Research Interests

The Morrison lab is interested in understanding molecular mechanisms of chromatin regulation, which are key in fundamental mechanisms of gene regulation and provide valuable insight into human health and disease. A complex network of machinery dynamically regulates the organization and accessibility of the human genome within chromatin. This re-organization starts at the level of the nucleosome, the basic subunit of chromatin. The nucleosome is a histone protein-DNA complex, and the N-terminal tails of the histone proteins protrude from the core complex to interact with regulatory machinery. These interactions are often driven by specific histone post-translational modifications (PTMs).

Our recent studies have contributed to recognizing that the histone tails have reduced accessibility to interactions with chromatin regulatory machinery within the nucleosome due to interactions with DNA. These findings suggest that there are other nuclear factors in vivo that modulate the conformation and in turn the accessibility of the tails to regulate interactions with protein machinery that lead to downstream chromatin regulation. We are taking a quantitative, biophysical approach in order to determine the role of the histone tails in chromatin structure and dynamics by studying the conformation and dynamics of the histone tails within nucleosomes. Factors such as histone PTMs and histone variants have the potential to directly regulate histone tail conformation, thereby regulating chromatin structure and modulating accessibility to binding factors.

The lab uses NMR spectroscopy along with a range of other biophysical and biochemical techniques in order to investigate these questions. If you are interested in joining the team, please contact Dr. Morrison.

Morrison et al., eLife, 2018