
Always supportive and deeply knowledgeable.
Polly Fordyce is an Associate Professor of Bioengineering and of Genetics and an Institute Scholar of the Sarafan ChEM-H Institute at Stanford University. She earned a B.A. in Physics and Biology from the University of Colorado at Boulder in 2000. She received her Ph.D. in Physics from Stanford University in 2007, working with Professor Steve Block on instrumentation and assays for single-molecule studies of kinesin motor proteins. Fordyce completed her postdoctoral training in Biophysics at the University of California, San Francisco in 2014 with Professor Joe DeRisi, where she developed microfluidic platforms to study transcription factor-DNA target recognition and bead-based multiplexing technologies.
The Fordyce Lab develops and applies microfluidic platforms for quantitative, high-throughput measurements of molecular interactions underlying cellular function. Key technologies include MITOMI and HT-MEK array-based devices with 1,568 reaction chambers for studying transcription factor binding and enzyme kinetics; MRBLEs, microspheres with over 1,000 distinct lanthanide ratios for spectral multiplexing; and Dropception for FACS-sortable double emulsion droplets enabling single-cell multi-omics. These tools provide kinetic and thermodynamic constants essential for biophysical models of protein-DNA, protein-protein, protein-peptide interactions, and enzymatic catalysis. Fordyce directs the Stanford Microfluidics Foundry since 2015 and serves as a Chan Zuckerberg Biohub Investigator since 2017. She has received the NIH Pioneer Award (2023-2028), New Innovator Award (2016-2021), NSF CAREER Award, 2023 Eli Lilly Award in Biological Chemistry, 2025 Schmidt Sciences Polymath Award, 2025 AAAS Fellowship, 2025 AIMBE Fellowship, and President's Award for Excellence Through Diversity (2024). Notable publications include 'Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics' (Science, 2021), 'De novo identification and biophysical characterization of transcription-factor binding sites with microfluidic affinity analysis' (Nature Biotechnology, 2010), 'Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro' (Nature Cell Biology, 2006), and 'Comprehensive, high-resolution binding energy landscapes reveal context dependencies of transcription factor binding' (PNAS, 2018). With over 4,600 citations, her innovations advance protein engineering, genomics, and biophysics.