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Structural Biophysics Laboratory (SBL)
Macromolecular NMR Section
R. Andrew Byrd, Ph.D.

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

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

  1. Ubiquitination
  2. Transcriptional Anti-termination
  3. Signal Transduction
    • Growth Factors
    • STAT Proteins
  4. NMR Methodology
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