R. Andrew Byrd, Ph.D.
Center for Structural Biology
Bldg. 538/Room 110 Frederick, MD 21702-1201
The Macromolecular NMR Section of the Center for Structural Biology (CSB) focuses on solution structural biology and biophysics aimed at understanding and regulating the mechanism of action, dynamics and complex formation of proteins and membrane surface signaling. The major structural tool is nuclear magnetic resonance (NMR) spectroscopy, and the group 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. Collaborations bring together our work with neutron reflectometry and molecular dynamics simulations. Research in the Byrd laboratory 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). In the Arf:ArfGAP system, we utilize nanodisc membrane mimetics to examine in situ membrane surface signaling. 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 2004-2021, chair of this committee 2015-2018, and on the Advisory Committee of the RCSB PDB 2009-2021.
Chao FA, Khago D, Byrd RA. Achieving pure spin effects by artifact suppression in methyl adiabatic relaxation experiments. J Biomol NMR. 2020;74(4-5):223-228.
Li J, Zhang Y, Soubias O, Khago D, Chao FA, Li Y, Shaw K, Byrd RA. Optimization of sortase A ligation for flexible engineering of complex protein systems. J Biol Chem. 2020;295(9):2664-2675.
Chao FA, Li Y, Zhang Y, Byrd RA. Probing the Broad Time Scale and Heterogeneous Conformational Dynamics in the Catalytic Core of the Arf-GAP ASAP1 via Methyl Adiabatic Relaxation Dispersion. J Am Chem Soc. 2019;141(30):11881-11891.
Li Y, Soubias O, Li J, Sun S, Randazzo PA, Byrd RA. Functional Expression and Characterization of Human Myristoylated-Arf1 in Nanodisc Membrane Mimetics. Biochemistry. 2019;58(10):1423-1431.
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.
Related Scientific Focus Areas
Biomedical Engineering and Biophysics
Molecular Biology and Biochemistry
This page was last updated on August 30th, 2021