Check out our ABB review on NMR of Intrinsically Disordered Proteins.
Nature Communications: Sequence-Specific Conformational Changes in RNA Pol II CTD.
Nature Communications: Conformational Heterogeneity in RNA Pol II CTD.
We apply biophysical chemistry techniques to understand the function of partially disordered proteins and to define the features of protein-RNA interactions. We are primarily Nuclear Magnetic Resonance (NMR) spectroscopists, but also feel that understanding biological chemistry requires the application of diverse techniques. NMR studies of protein dynamics combined with computational and theoretical studies of the coupling between nuclear spin relaxation and molecular motion provide a complete picture of protein structure. Emphasis is placed on biophysical studies of macromolecular interactions involving partially disordered proteins and/or protein-RNA interactions in order to build the connection with function. We wish to understand the functional implications of protein dynamics and disorder in protein mediated signaling and other biological events. For details, please click the Research link above.
The Showalter Laboratory is proud to be a part of the Center for Eukaryotic Gene Regulation (CEGR). The research interests of all CEGR members are focused on understanding the mechanisms of gene regulation, although each member brings unique perspectives and expertise. What this means for trainees in the Showalter Laboratory and for our science is a world-class, immersive, and multi-disciplinary environment in which we apply the tools and theories we love toward biological and biomedical advances in gene regulation.The CEGR is the recipient of an NIH predoctoral training grant in eukaryotic gene regulation.
This website is nearly complete, but still under construction. If you are looking for something you cannot find, our previous website can still be found here.