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R. Andrew Byrd, PhD
Head, Macromolecular NMR Section
Building 538, Room 120
Frederick, MD 21702-1201
Macromolecular NMR (MNMR) Section
Our lab is interested in the structural biology and biophysics of proteins involved in signal transduction, transcriptional regulation, and protein degradation. We utilize nuclear magnetic resonance (NMR) spectroscopy to study the three-dimensional (3D) structures of proteins, protein:protein complexes, and protein:nucleic acid complexes. We employ the full range of state-of-the-art multi-nuclear NMR methods, including residual dipolar coupling, paramagnetic relaxation enhancement, and pseudocontact shift parameters. We also incorporate a range of biophysics measurements into these studies, including isothermal calorimetry (ITC), fluorescence polarization, analytical ultracentrifugation, light scattering, and small angle X-ray scattering (SAXS and WAXS). By combining all of these tools, we incorporate a sound structural understanding into the elucidation and modulation of biological mechanisms in collaboration with biologists within the CCR and the extramural community.
- Ubiquitination Pathway and ERAD
- Transcriptional Anti-Termination
- Signal Transduction - STAT Proteins
- NMR Methodology