Macromolecular NMR Section
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R. Andrew Byrd, Ph.D.
Head, Macromolecular NMR Section
Building 538, Room 120
Frederick National Lab
Frederick, MD 21702-1201
Phone: 301-846-1407
Fax: 301-846-6231
E-Mail: byrdra@mail.nih.gov
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Introduction
Our lab is interested in the structural biology and biophysics of proteins involved
in signal transduction and protein degradation. These areas of interest naturally
lead to the study of multi-component complexes and the understanding of the interactions
between these molecules that drive the function. We utilize NMR spectroscopy to
study the three-dimensional 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. Working in collaboration with our colleague
Yun-Xing Wang Head, PNAI Section, SBL, we use solution small-angle X-ray scattering (SAXS) in combination
with our NMR methods to determine structures and interactions in multi-component
complexes. We also incorporate a range of biophysics measurements into these studies,
including isothermal calorimetry (ITC), fluorescence polarization, analytical ultracentrifugation,
and light scattering. 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.
Research Projects
- Ubiquitination
- Transcriptional Anti-termination
- Signal Transduction
- Growth Factors
- STAT Proteins
- NMR Methodology