Department Faculty

Gerard Marriott

Professor, Department of Bioengineering
274 Hearst Memorial Mining Building
mailcode: 1762

Research Interests

The Marriott laboratory seeks to understand the molecular and structural basis of complex cellular processes including motility and muscle contraction. These studies borrow concepts and principles from chemistry, biology, engineering and physics for the design and application of new optical probes and microscope imaging techniques that are used to investigate protein function and dynamics over a hierarchy of organizational levels, ranging from single molecules to cells within animals.


1990~1992   Postdoc., Keio University, Physics

1987~1989   Postdoc., Max Planck Institute for Biophysical Chemistry, Biophysics

1987             Ph.D., University of Illinois, Biochemistry

1980             B.Sc. (Hons).,  Birmingham University, UK, Biochemistry

Major Awards

Fluorescence Investigator Award. American Biophysics Society

Japan Society for the Promotion of Science Fellow

Top-ten Innovations of 2008 for OLID-FRET - The Scientist magazine

Alexander von Humboldt Society Fellow.

Professional Experience

1999-present      Faculty Scientist, Computational and Theoretical Biology Department, Physical Biosciences Division, Lawrence Berkeley National Laboratory

Current Information:

2009-present: Professor, Department of Bioengineering, UC-Berkeley

2009-present   Faculty Scientist, Physical Biosciences Division, Lawrence Berkeley National Laboratory

2005-2009   Professor, Department of Physiology, University of Wisconsin-Madison

2010-present   Guest Professor. Tsinghua University Graduate School, Shenzhen, China

2006-present   Guest Professor. Department of Bioengineering, SouthEast University, Nanjing, China

2005-2006       Visiting Professor, Department of Biochemistry, Stanford University

1999-2005       Associate Professor, Dept. of Physiology, University Wisconsin-Madison

1992-1999       C3 Professor (nachwuchsgruppenleiter), Max Planck Institute for Biochemistry, Martinsried, Germany

Selected Publications

1. Wu, L, Dai, YR and Marriott, G. (2011). Optical Control of Calcium Affinity in a Spiroamido-rhodamine Based Calcium Chelator, Chem. Letters. In press

2. Yan, Y., Marriott, M.E., Petchprayoon, C. and Marriott, G. (2011). Optical switches: High-contrast imaging in living cells and tissue. Biochemical Journal. 433 (411–422).

3. Yan, Y. and Marriott, G. (2011). Optical Manipulation of Protein Activity and Protein Interactions Using Caged Proteins and Optical Switch Protein Conjugates. In: Photo-control of Biological Function. Eds. Chambers, J. and Kramer, R. Elsevier Protocols. Humana Press. pp. 213-231

4. Petchprayoon, C. and Marriott, G. (2010). Synthesis and spectroscopic characterization of red-shifted spironaphthoxazine optical switch reagents for studies in living cell. Tetrahedron Letters. doi:10.1016/j.tetlet.2010.10.084

5. Petchprayoon, C, Yan, Y., Mao, S. and Marriott, G. (2010). Rational design, synthesis and characterization of highly fluorescent optical switches for high-contrast optical lock-in detection (OLID) imaging microscopy in living cells. Bioorganic and Medicinal Chemistry. doi:10.1016/j.bmc.2010.07.015

6. Marriott, G., Mao, S., T. Sakata, Jackson, D. Gomez, T., Aaron, H., Isacoff, EY, Yan, Y. High contrast imaging based on optical lock-in detection imaging of synthetic and genetically encoded optical switches:. PNAS (USA). 105:17789-17794

7. Perrins, RD, Cecere, G., Paterson I. and Marriott, G. (2008). Molecular Dissection and Functional Analysis of Reidispongiolide A binding to actin.Chemistry and Biology, 15, 287-294

8. Mao, S., Benninger, RKW., Piston, D., Jackson, Easley, C., D. Yan, Y. & Marriott, G. (2008). Optical lock-in detection of FRET using genetically encoded optical switches: High contrast FRET imaging of protein interactions in living cells. Biophysical J. 94, 4515–4524

9. Wang, H, Mao, S., Chalovich, J. & Marriott, G. (2008). Tropomyosin dynamics in cardiac thin filaments: A multi-site Foerster resonance energy transfer and anisotropy study. Biophysical J. 94. 4358–4369