Joseph H. Schmidt

This paper computationally designs light-responsive proteins that undergo conformational changes upon light activation, enabling precise control of biological functions.

This study designs metamorphic proteins that switch between multiple conformations and shows how mutations can shift their conformational equilibrium.

This paper introduces LDDM, a generative model for drug design that produces synthetically accessible compounds validated experimentally for five protein targets.

This study designs polymorph-specific binders for α-synuclein fibrils using a computational pipeline, demonstrating their utility as selective labeling agents without interfering with fibril dynamics.

The paper identifies 4,500 targetable sites on the human surfaceome and introduces binder seeds for protein design, validated through experimental approaches and supported by a database.

This paper introduces DiffTopo, a diffusion model for generating novel protein folds, and MirrorTopo, a pipeline to expand known fold space by mirroring native protein topologies.

The paper develops caffeine-inducible systems for controlling gene expression in human cells using humanized protein components and demonstrates their use in inducible gene expression in T-cells.

This paper designs proteins that target neosurfaces from protein-ligand complexes using a deep learning approach, validated experimentally against three drug-bound protein complexes.

This paper designs chimeric influenza hemagglutinins that combine antigenic surfaces from different strains to elicit cross-group immunity and neutralize multiple strains.

Hallucinating binders by backpropagating through AlphaFold2 weights gave, across 12 targets, binders in 10-100% of the designs tested per target, mostly at nanomolar affinity.