Steven G. Boxer
Department of Chemistry
Stanford University
Stanford, California 94305

(650) 723-4482

sboxer@stanford.edu

www.stanford.edu/group/boxer

University of Chicago
Degree: Ph.D. December 1976
Field: Physical and Physical-Organic Chemistry
Research Advisor: Professor Gerhard L. Closs

Tufts University
Degree: B.S. with Honors, June 1969
Major: Chemistry

33rd Musselman Lecture Series, Gettysburg College, November 2011

Peter C. Reilly Lectures, Notre Dame, April 2010

Moses Gomberg Lecture, University of Michigan, May 2009

The James D. and Julia P. Morrison Lecture, Carleton College, April 2008

Hirschmann Lectures, University of Pennsylvania, March 2008

Craig Lecturer, Research School of Chemistry, Canberra, November 2007

Max Tishler Award Lecturer, Tufts University, March 2007

J. Clarence Karcher Lecturer, University of Oklahoma, March 2006

Henry Bull Lecturer in Biophysics, University of Iowa, April 2004

ICI Distinguished Lecturer, University of Calgary, Calgary, Canada, October 2003

Merck Lecturer, University of California, San Diego, May 2002

Ehrenfest Colloquium, University of Leiden, May 2001

H. Willard Davis Lecture, University of South Carolina, Columbia South Carolina, March 1998.

Five-College Lecturer in Chemistry, Amherst, Hampshire, Mount Holyoke and Smith Colleges and the University of Massachusetts, April, 1993.

Physical Sciences Colloquium, IBM J. T. Watson Research Laboratories, Yorktown Heights, New York, October, 1990.

Dr. George W. Raiziss Biochemical Rounds, University of Pennsylvania, Department of Biochemistry and Biophysics, April, 1987.

Weissberger-Williams Lecturer, Eastman Kodak Company, Rochester, New York, March, 1988

Ephriam and Wilma Shaw Roseman Lecturer, Department of Chemistry, Johns Hopkins University, Baltimore, November, 1987.

Current:

Scientific advisory board, Synamem

Scientific advisory board, Applied Nanosystems, B.V.

PULSE External Advisory board, SLAC

Former:

Samsung Advanced Institute of Technology (2005–2008)

External Advisory Board, CSEM-MRSEC Caltech (2001–2005)

Scientific Review Board, Howard Hughes Medical Institute (1998–2006)

Scientific Review Board, Member NIH Study Section, BBCB (2000–2004)

Scientific advisory board, MCM Laboratories

Scientific advisory board, Salutar, Inc.

Scientific advisory board, Pharmacyclics, Inc.

Scientific advisory board, Signature BioSciences, Inc.

Scientific advisory board, ACLARA BioSciences, Inc.

Consultant, Darwin Molecular Technology, Inc.

Consultant, Polaroid

Chemical Physics (1992–)

Journal of Physical Chemistry (1994–2005)

Physical Chemistry Chemical Physics (2002–2004)

Advanced Functional Materials (2001–2004)

Accounts of Chemical Research (1997–2000)

Annual Reviews of Biophysics and Biomolecular Structure (1994–2001)

Biophysical Journal (1994–2000)

Journal of Biological Inorganic Chemistry (1996–1998)

Spectrochemica Acta (1994–2000)

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.

A third major area of interest involves the use of 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 research page for more information.