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Nuclear Magnetic Resonance Group

NMR & Ligand-Macromolecule Interactions

Robert London, Ph.D.
Robert London, Ph.D.
Principal Investigator
Tel (919) 541-4879
Fax (919) 541-5707
london@niehs.nih.gov
P.O. Box 12233
Mail Drop MR-01
Research Triangle Park, North Carolina 27709
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NMR & Ligand-Macromolecule Interactions
A computer-generated model depicting the structure of a protein.

Research Summary

The Nuclear Magnetic Resonance (NMR) Group performs fundamental research on biological systems aimed at providing insight into the molecular mechanisms that underlie problems of environmental concern. As part of the Laboratory of Structural Biology, our primary focus has been the evaluation of structural, conformational and dynamic responses of proteins to substrates, cofactors, allosteric effectors, other proteins, putative environmental toxins, nucleic acids, etc.

 

Major areas of research:

  • DNA repair complexes
  • HIV reverse transcriptase
  • Structural characterization of allergens

 

Current projects:

  • Structural and dynamic characterization of enzymes involved in DNA polymerization
  • Studies of nucleases, particularly focused on the proofreading exonuclease of E. coli and on the ribonuclease H domain of HIV reverse transcriptase
  • Analysis of ligand-macromolecule complex formation and related ternary complex formation (studies of borate complexes; studies of Type II dihydrofolate reductase)

 

Robert London, Ph.D., heads the Nuclear Magnetic Resonance Group within the Laboratory of Structural Biology. He received his Ph.D. in biophysics from the University of Illinois in 1973. He has published over 200 peer-reviewed articles in leading biomedical journals, and contributed 20 book chapters. He served as principal investigator of the NIH-funded National Stable Isotope Resource at Los Alamos before joining NIEHS in 1983.


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