Bob London, Ph.D.

Senior Investigator

Genome Integrity & Structural Biology Laboratory / Nuclear Magnetic Resonance Group


MRI-08 Rall Building
111 T W Alexander Dr
Research Triangle Park, NC 27709


Research Topics

The ability of cells to function and to survive is dependent on biological catalysts that facilitate the transformation of available nutrients into cellular components, metabolize fats and carbohydrates to obtain energy, and sustain a multitude of cellular functions. These catalysis are predominantly proteins ñ sequences of amino acids, that adopt three dimensional structures allowing them to recognize their target substrate molecules, and to optimize the conversion of the target to a specific product with extremely high efficiency. Determining the three dimensional shapes of these biological catalysts is an essential step in understanding their function. For catalytic enzymes, this determination reveals the structural and functional significance of each component amino acid. This information is central to understanding how this function can be impaired in various disease states, or in the presence of harmful environmental agents.


Dr. London received his PhD in physical biochemistry from the University of Illinois in 1973. He was subsequently a postdoctoral fellow and later a staff scientist in the Stable Isotopes (ICONS) Program of the Los Alamos National Laboratory. This program, which later received additional support from the NIH to form the National Stable Isotopes Resource, facilitated the introduction of stable isotopes of carbon, nitrogen, and oxygen in basic biochemical and biomedical research. Dr. London moved to the NIEHS in 1983 to become Principal Investigator of the NMR research group in the Laboratory of Molecular Biophysics, and subsequently the Laboratory of Structural Biology.

Selected Publications

  1. London RE. Theoretical analysis of the inter-ligand overhauser effect: a new approach for mapping structural relationships of macromolecular ligands. J Magn Reson. 1999;141(2):301-11.

  2. Cuneo MJ, London RE. Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity. Proc Natl Acad Sci U S A. 2010;107(15):6805-10.

  3. Zheng X, Perera L, Mueller GA, DeRose EF, London RE. Asymmetric conformational maturation of HIV-1 reverse transcriptase. Elife. 2015;4.

  4. Kirby TW, Gassman NR, Smith CE, Zhao ML, Horton JK, Wilson SH, London RE. DNA polymerase β contains a functional nuclear localization signal at its N-terminus. Nucleic Acids Res. 2017;45(4):1958-1970.

  5. London RE, Wingad BD, Mueller GA. Dependence of amino acid side chain 13C shifts on dihedral angle: application to conformational analysis. J Am Chem Soc. 2008;130(33):11097-105.

This page was last updated on April 12th, 2013