R. Andrew Byrd, Ph.D.
Center for Structural Biology
Bldg. 538/Room 110
Frederick, MD 21702-1201
The Structural Biophysics Laboratory (SBL) focuses on solution structural biology and biophysics aimed at understanding and regulating the mechanism of action of proteins and nucleic acids. The major structural tool for the SBL is nuclear magnetic resonance (NMR) spectroscopy, and the Laboratory has a very strong interdisciplinary approach to understanding biochemical and biological mechanisms. Technologies incorporated in the research program include solution X-ray scattering, fluorescence and circular dichroism spectroscopy, mass spectrometry, calorimetry and novel binding methodologies including SPR and microscale thermophoresis. Research in the Byrd laboratory (Macromolecular NMR Section) focuses on protein-protein interactions in the ubiquitin-proteasome regulation pathway and the area of ADP-ribosylation factor (Arf) family of GTP-binding proteins and their regulators, the Arf GTPase-activating proteins (Arf GAPs). We seek to provide detailed structural and mechanistic insight, which we combine with collaborations in molecular and cell biology to inform and modulate biological function
Dr. Byrd received his Ph.D. from the University of South Carolina, specializing in high-resolution biomolecular NMR. He was a postdoctoral fellow and subsequently a research officer in the Molecular Biophysics Laboratory of the National Research Council of Canada, where he investigated biological membranes by solid-state NMR. Following a period as a senior investigator at the Center for Drugs and Biologics/FDA, he established the Macromolecular NMR Section of the ABL-Basic Research Program at the NCI-Frederick in 1992. He chaired the Experimental NMR Conference in 1992 and co-chaired the International Conference on Magnetic Resonance in Biological Systems in 1996. Dr. Byrd served as Chief of the Structural Biophysics Laboratory in the Center for Cancer Research, NCI from 1999-2017. He has served on multiple drug discovery panels for NCI and served as the Director of the Molecular Discovery Program from 2009-2011. Dr. Byrd continues his work as a Senior Investigator in the Center for Structural Biology. He has been very active with the Protein Data Bank (PDB), serving on the Advisory Committee of the world-wide PDB 2004-present, chair of this committee 2015-2018, and on the Advisory Committee of the RCSB PDB since 2009.
Chakrabarti KS, Li J, Das R, Byrd RA. Conformational Dynamics and Allostery in E2:E3 Interactions Drive Ubiquitination: gp78 and Ube2g2. Structure. 2017;25(5):794-805.e5.
Chao FA, Byrd RA. Geometric Approximation: A New Computational Approach To Characterize Protein Dynamics from NMR Adiabatic Relaxation Dispersion Experiments. J Am Chem Soc. 2016;138(23):7337-45.
Das R, Liang YH, Mariano J, Li J, Huang T, King A, Tarasov SG, Weissman AM, Ji X, Byrd RA. Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine. EMBO J. 2013;32(18):2504-16.
Cecchi F, Pajalunga D, Fowler CA, Uren A, Rabe DC, Peruzzi B, Macdonald NJ, Blackman DK, Stahl SJ, Byrd RA, Bottaro DP. Targeted disruption of heparan sulfate interaction with hepatocyte and vascular endothelial growth factors blocks normal and oncogenic signaling. Cancer Cell. 2012;22(2):250-62.
Das R, Mariano J, Tsai YC, Kalathur RC, Kostova Z, Li J, Tarasov SG, McFeeters RL, Altieri AS, Ji X, Byrd RA, Weissman AM. Allosteric activation of E2-RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78. Mol Cell. 2009;34(6):674-85.
Related Scientific Focus Areas
Biomedical Engineering and Biophysics
Molecular Biology and Biochemistry
This page was last updated on December 7th, 2020