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R. Andrew Byrd, Ph.D.

Portait Photo of R. Andrew Byrd
Structural Biophysics Laboratory
Head, Macromolecular NMR Section
Laboratory Chief
Center for Cancer Research
National Cancer Institute
Building 538, Room 120
P.O. Box B
Frederick, MD 21702-1201
Phone:  
301-846-1407
Fax:  
301-846-6231
E-Mail:  
byrdra@mail.nih.gov

Biography

Dr. Byrd received his Ph.D. from the University of South Carolina in 1977, 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 has been the Chief of the Structural Biophysics Laboratory in the Center for Cancer Research, NCI since 1999. He has served on multiple drug discovery panels for NCI and served as the Director of the Molecular Discovery Program from 2009-2011.

Research

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

This page was last updated on 11/18/2013.