W. E. (William Esco) Moerner, the Harry S. Mosher Professor of Chemistry and Professor by courtesy of Applied Physics, has conducted research in physical chemistry, biophysics, and the optical properties of single molecules, and is actively involved in the development of 2D and 3D super-resolution imaging for cell biology. Imaging studies include protein superstructures in bacteria, structure of proteins in cells, studies of chromatin organization, and dynamics of regulatory proteins in the primary cilium. Using powerful microscopes optimized for tracking of single objects in cells, the motions of proteins, DNA, and RNA are being measured in three dimensions in real time to understand processing and binding interactions. A related research area concerns precise analysis of photodynamics of single trapped biomolecules in solution, with applications to photosynthesis, protein-protein interactions, and transport measurements.
Born on June 24, 1953 at Parks Air Force Base in Pleasanton, California, Professor Moerner was raised in San Antonio, Texas. He attended Washington University as a Langsdorf Engineering Fellow, graduating in 1975 with degrees in Physics and Electrical Engineering (both B.S. with top honors), and Mathematics (A.B. summa cum laude). His doctoral research in physics at Cornell University (M.S. 1978, Ph.D. 1982) employed tunable infrared lasers to explore infrared vibrational modes of impurities in crystals. In 1982, he moved from New York to San Jose, California to join the IBM Research Division developing spectral holeburning for frequency domain optical storage and photorefractivity for dynamic hologram formation. After 13 years at IBM, Dr. Moerner accepted a position as Distinguished Professor of Physical Chemistry at UC San Diego, where he broadened his research to include biological systems and biophysics. Recruited to the Stanford Chemistry Department faculty in 1997, he served as Chair of the department from 2011 to 2014.
Professor Moerner’s scientific contributions were recognized with the 2014 Nobel Prize in Chemistry "for the development of super-resolved fluorescence microscopy." One method to surpass the optical diffraction limit (PALM/STORM) uses single-molecule imaging combined with a control mechanism to keep the concentration of emitting molecules at a very low level, followed by sequential localization to reconstruct the underlying structure. The fundamentals of this idea came from early work in the Moerner lab: optical detection and imaging of single molecules (1989) combined with blinking and switching at low temperature, as well as the discovery of optical control of single copies of green fluorescent protein at room temperature (1997). Among many other honors and awards, Professor Moerner was elected fellow of the American Physical Society, Optical Society of America, American Association for the Advancement of Science, American Academy of Arts and Sciences; and member of the National Academy of Sciences.
Today, the Moerner Laboratory uses laser spectroscopy and microscopy of single molecules to probe biological processes, one molecule at a time. Primary thrusts include development and application of fluorescence microscopy far beyond the optical diffraction limit by PALM/STORM and STED approaches, single-molecule tracking in complex cellular environments, invention and validation of methods for precise and accurate 3D optical microscopy in cells, and trapping of single photosynthetic biomolecules in solution for extended study. Through a variety of collaborations, these approaches are applied to explore protein and oligonucleotide localization patterns in bacteria, measure structures of amyloid aggregates in cells, define the behavior of signaling proteins in the primary cilium, quantify photodynamics for photosynthetic proteins and enzymes, and observe the dynamics of DNA and RNA in cells and viruses.
Please visit the Moerner Lab home page for more information.
Gustavsson, A.-K., Petrov, P. N., Lee, M. Y., Shechtman, Y., & Moerner, W. E. (2018). 3D single-molecule super-resolution microscopy with a tilted light sheet. NATURE COMMUNICATIONS, 9, 123.
Conley, N. R., Dragulescu-Andrasi, A., Rao, J., & Moerner, W. E. (2012). A Selenium Analogue of Firefly D-Luciferin with Red-Shifted Bioluminescence Emission. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 51(14), 3350–53.
Ptacin, J. L., Lee, S. F., Garner, E. C., Toro, E., Eckart, M., Comolli, L. R., … Shapiro, L. (2010). A spindle-like apparatus guides bacterial chromosome segregation. NATURE CELL BIOLOGY, 12(8), 791–U46.
Ptacin, J. L., Gahlmann, A., Bowman, G. R., Perez, A. M., von Diezmann, A. R. S., Eckart, M. R., … Shapiro, L. (2014). Bacterial scaffold directs pole-specific centromere segregation. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 111(19), E2046–E2055.
Sahl, S. J., Weiss, L. E., Duim, W. C., Frydman, J., & Moerner, W. E. (2012). Cellular Inclusion Bodies of Mutant Huntingtin Exon 1 Obscure Small Fibrillar Aggregate Species. SCIENTIFIC REPORTS, 2.
Backlund, M. P., Joyner, R., & Moerner, W. E. (2015). Chromosomal locus tracking with proper accounting of static and dynamic errors. PHYSICAL REVIEW E, 91(6).
Backlund, M. P., Joyner, R., & Moerner, W. E. (2015). Chromosomal locus tracking with proper accounting of static and dynamic errors. Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics, 91(6), 062716-?
Bockenhauer, S., Fürstenberg, A., Yao, X. J., Kobilka, B. K., & Moerner, W. E. (2011). Conformational dynamics of single G protein-coupled receptors in solution. Journal of Physical Chemistry. B, 115(45), 13328–38.
Backlund, M. P., Joyner, R., Weis, K., & Moerner, W. E. (2014). Correlations of three-dimensional motion of chromosomal loci in yeast revealed by the double-helix point spread function microscope. Molecular Biology of the Cell, 25(22), 3619–29.
Sahl, S. J., Lau, L., Vonk, W. I. M., Weiss, L. E., Frydman, J., & Moerner, W. E. (2016). Delayed emergence of subdiffraction-sized mutant huntingtin fibrils following inclusion body formation. Quarterly Reviews of Biophysics, 49.