Steven Boxer

About

Steven Boxer is the Camille Dreyfus Professor of Chemistry at Stanford University. He earned his PhD from the University of Chicago in 1976, specializing in Physical and Physical-Organic Chemistry, and his BS with Honors in Chemistry from Tufts University in 1969. His laboratory investigates the structure and function of biological systems through a physical perspective, developing experimental methods and theories as needed. His research encompasses several interconnected themes, including the excited state dynamics in Green Fluorescent Protein (GFP) and split GFP, where his team demonstrated the existence of two protonation states of the GFP chromophore that interconvert via ultrafast excited state proton transfer. This work has led to the development of GFP variants with diverse colors and sensitivities. His group also explores the optogenetic applications of split GFPs, which can be photodissociated or associated with peptides using light. Additionally, Boxer studies electrostatics and dynamics in proteins, utilizing Stark spectroscopy and vibrational probes to measure electrostatic fields within proteins and their influence on enzymatic activity. His research extends to model membranes, where supported lipid bilayers serve as mimics for cell surfaces, enabling the study of membrane organization, fusion, and protein interactions. His work in energy and electron transfer in photosynthesis involves femtosecond spectroscopy and mutagenesis to understand electron transfer…

Research topics

• Stereochemistry
• Quantum mechanics
• Chemical physics
• Computational chemistry
• Organic chemistry
• Atomic physics
• Chemistry
• Physics

Selected publications

• Electrostatic control of photoisomerization pathways in proteins

  Science · 2020-01-02 · 114 citations

  articleOpen accessSenior authorCorresponding

  Rotation around a specific bond after photoexcitation is central to vision and emerging opportunities in optogenetics, super-resolution microscopy, and photoactive molecular devices. Competing roles for steric and electrostatic effects that govern bond-specific photoisomerization have been widely discussed, the latter originating from chromophore charge transfer upon excitation. We systematically altered the electrostatic properties of the green fluorescent protein chromophore in a photoswitchab…

  PublisherOA PDFDOI

• Membrane-tethered mucin-like polypeptides sterically inhibit binding and slow fusion kinetics of influenza A virus

  Proceedings of the National Academy of Sciences · 2020-05-26 · 89 citations

  articleOpen access

  The mechanism(s) by which cell-tethered mucins modulate infection by influenza A viruses (IAVs) remain an open question. Mucins form both a protective barrier that can block virus binding and recruit IAVs to bind cells via the sialic acids of cell-tethered mucins. To elucidate the molecular role of mucins in flu pathogenesis, we constructed a synthetic glycocalyx to investigate membrane-tethered mucins in the context of IAV binding and fusion. We designed and synthesized lipid-tethered glycopoly…

  PublisherOA PDFDOI

• A two-directional vibrational probe reveals different electric field orientations in solution and an enzyme active site

  Nature Chemistry · 2022-05-05 · 79 citations

  articleOpen accessSenior author
  PublisherOA PDFDOI

• A Preorganized Electric Field Leads to Minimal Geometrical Reorientation in the Catalytic Reaction of Ketosteroid Isomerase

  Journal of the American Chemical Society · 2020 · 66 citations

  Senior authorCorresponding

  Electrostatic interactions play a pivotal role in enzymatic catalysis and are increasingly modeled explicitly in computational enzyme design; nevertheless, they are challenging to measure experimentally. Using vibrational Stark effect (VSE) spectroscopy, we have measured electric fields inside the active site of the enzyme ketosteroid isomerase (KSI). These studies have shown that these fields can be unusually large, but it has been unclear to what extent they specifically stabilize the transiti…

  DOI

• Beyond the Vibrational Stark Effect: Unraveling the Large Redshifts of Alkyne C–H Bond in Solvation Environments

  Journal of the American Chemical Society · 2025-02-10 · 12 citations

  articleOpen accessSenior authorCorresponding

  C–H···O hydrogen bonds are formed in systems ranging from biomolecular complexes to small-molecule structures. Previous work has focused on the blueshifts in the C–H stretching frequency (ν¯CH) induced by these hydrogen bonds and their chemical and biological roles. Here, we show that, in contrast, terminal alkyne C–H hydrogen bonds exhibit large redshifts (50–100 cm–1) upon hydrogen bonding with oxygen-containing solvents. Using spectroscopic and computational approaches, we elucidate and compa…

  PublisherOA PDFDOI

Recent grants

• Organization and Dynamics in Photosynthetic Reaction Centers and Model Membrane Architectures

  NSF · $1.4M · 2014–2019

• Mechanism and Macromolecular Organization in Photosynthetic Reaction Centers

  NSF · $931k · 2004–2010

• Organization and Dynamics in Photosynthetic Reaction Centers and Model Membrane Architectures

  NSF · $1.2M · 2019–2024

Frequent coauthors

• Seth R. Marder

  86 shared

• Stefan Franzen

  North Carolina State University

  85 shared

• William H. Woodruff

  University of Illinois Urbana-Champaign

  60 shared

• Gerold U. Bublitz

  Stanford University

  58 shared

• S. James Remington

  University of Oregon

  41 shared

• Melissa Thomas

  40 shared

• G. I. Stegeman

  King Fahd University of Petroleum and Minerals

  36 shared

• Jun Li

  36 shared

Similar researchers at Stanford University

• Carolyn Bertozzih-190
• Richard Zareh-139
• Robert Waymouthh-101