Skip to Content
Assistant Professor of Biochemistry
Primary Office: 4-452 BSBIowa City, IA 52242
Email: email@example.comWeb: Musselman Laboratory
BS, Chemistry, University of Colorado at DenverMS, Chemistry, University of MichiganPhD, Chemistry, University of Michigan
Fellowship, Chemistry, University of Colorado, Denver School of Medicine
Department of Biochemistry PhD
The genome of every eukaryotic cell resides in complex with histone proteins to form chromatin. Though originally thought to just package the genome into the nucleus, chromatin structure is now recognized to play an active role in the regulation of all DNA templated processes in eukaryotes. Such regulation requires the spatial and temporal alteration of chromatin structure, which is mediated by the chemical modification of histones and DNA as well as by the action of a large number of chromatin associated cofactors. My lab is interested in deciphering mechanisms of chromatin structure modulation and how misregulation of these pathways is associated with disease. Specifically, our goal is to elucidate, on the molecular level, the details of how cofactors target nucleosomes, especially in response to histone modification, and how this leads to the regulation of genes. Such knowledge will enhance our fundamental understanding of chromatin biology as well as reveal the etiology of many human diseases with the aim of eventually aiding in the development of targeted therapeutics. We employ NMR spectroscopy, X-ray crystallography as well as a variety of other biophysical and biochemical techniques to approach these questions.
Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1..
Structure (London, England : 1993).
2015 February 3. 23(2):312-21.
Inhibition of histone binding by supramolecular hosts..
Photoactive Spatial Proximity Probes for Binding Pairs with Epigenetic Marks.
J Photochem Photobiol A Chem.
The structural basis of urea-induced protein unfolding in β-catenin.
Acta Crystallogr D Biol Crystallogr.
Towards understanding methyllysine readout.
Biochim Biophys Acta.
Binding of PHF1 Tudor to H3K36me3 enhances nucleosome accessibility.
Perceiving the epigenetic landscape through histone readers.
Nature structural & molecular biology.
2012 December. 19(12):1218-27.
Molecular basis for H3K36me3 recognition by the Tudor domain of.
Natural Structure Molecular Biology.
2012 November 11. 19:1266-1272.
Mi-2/NuRD chromatin remodeling complexes maintain transcriptional attenuation during B cell development.
Journal of Immunology.
2012 May 1. 188.
Bivalent Recognition of a Single Nucleosome by the Tandem PHD Fingers of CHD4 is Required for CHD4-Mediated Repression.
2012 January 31. 102(3):480a.
Date Last Modified: 06/06/2016 -
Copyright © 2015 The University of Iowa. All Rights Reserved.