Camille and Henry Dreyfus Professor of Chemistry (b. 1947)
B.S., 1969,
Tufts University; Ph.D., 1976, University of Chicago
A.P. Sloan Fellow,
1980; Dreyfus Teacher-Scholar Fellow, 1981; Dean's Award for Distinguished
Teaching, 1982; Presidential Young Investigator Award, 1984; American Society of
Photobiology Award, 1992; Five College Lecturer in Chemistry, 1993; NIH Merit
Award, 1994; ACS Cope Scholar Award, 1995; American Academy of Arts and
Sciences, 1997
Physical, Biophysical Chemistry; Bio-nanotechnology
650-723-4482
sboxer@stanford.edu
Boxer Group
My laboratory investigates the structure and function of biological systems using many tools and methods, always with a strong physical perspective. Three interconnected themes are being pursued.
First, we have a long-standing interest in the mechanism of light-driven long-distance electron transfer in photosynthetic reaction centers, one of the fastest known reactions. This is being studied by femtosecond fluorescence and transient absorption spectroscopy, manipulation in electric fields, site-specific mutagenesis and some novel types of Stark spectroscopy we have developed and applied to many types of molecules. Related methods are also being used to probe excited state dynamics and electronic structure in variants of green fluorescent protein (GFP), widely used in cell biology.
Second, we are broadly interested in electrostatics in proteins and how electrostatics affects function. Our current work uses probes whose sensitivity to electric fields can be calibrated by Stark spectroscopy. Vibrational Stark experiments are particularly useful as they provide a calibration for mapping electrostatic fields in proteins. Probes have also been developed that can measure the time-dependent solvation of charges at different positions in proteins, a key aspect of protein-protein and protein-ligand interactions and catalysis. These approaches are also being used to investigate photosynthetic reaction centers and GFP.
Third, we use supported lipid bilayers as mimics for cell surfaces and as tools in biotechnology. A broad vision is to engineer interfaces between hard surfaces and soft materials, ultimately leading to sophisticated biocompatible interfaces that can be used to control, interrogate or organize complex living systems. We have developed methods for partitioning and manipulating the composition and organization of these unique self-assembled systems. Recent work addresses the formation of domains and protein association with these domains, interactions of DNA, proteins and cells with supported bilayers, and the mechanism of vesicle fusion, both to solid supports and mediated by proteins. This work has motivated the development of advanced optical microscopy methods for probing the interface between membranes on solid supports and cell membranes, potentially with nm vertical resolution. A novel type of imaging mass spectrometry is being applied to characterize the lateral organization and composition of bilayers and associated membranes with 50 nm resolution.Please visit our web site for more information.
1 "Vibrational Stark Effects Calibrate the Sensitivity of Possible Probes of Electric Fields in Proteins," I. Suydam and S.G. Boxer, Biochemistry, 42, 12050-12055 (2003).
2 “A Theory of Intervalence Band Stark Effects,” T.P. Treynor and S.G. Boxer, Journal of Physical Chemistry A, 108, 1764-1778 (2004).
3 “Green Fluorescent Protein Variants as Ratiometric Dual Emission pH Sensors: 3. Temperature Dependence of Proton Transfer,” T.B. McAnaney, X. Shi, P. Abbyad, H. Jung, S.J. Remington and S.G. Boxer, Biochemistry, 44, 8701-8711 (2005).
4 “Supported Membrane Composition Analysis by Secondary Ion Mass Spectrometry with High Lateral Resolution,” C. Galli Marxer, M.L. Kraft, P.K. Weber, I.D. Hutcheon and S.G. Boxer, Biophysical Journal, 88, 2965-2975 (2005).
5 “Controlling Two-dimensional Tethered Vesicle Motion Using an Electric Field: Interplay of Electrophoresis and Electro-osmosis”, Chiaki Yoshina-Ishii and Steven G. Boxer”, Langmuir, 22 , 2384-2391 (2006).
6 “High Yield of M-Side Electron Transfer in Mutants of Rhodobacter capsulatus Reaction Centers Lacking the L-side Bacteriopheophytin”, J. I. Chuang, S. G. Boxer, Dewey Holten and Christine Kirmaier, Biochemistry (Accelerated Publication), 45, 3845-3851 (2006).