REVIEW 2 cited by
Protein Discovery with Discrete Walk-Jump Sampling
Not yet reviewed by Pith; the record is open.
This paper has not been read by Pith yet. Machine review is queued; the pith claim, tier, and objections will appear here once it completes.
SPECIMEN: schema-true, not a live event
T0 review · schema-true
One-sentence machine reading of the paper's core claim.
pith:XXXXXXXX · record.json · timestamp
read the original abstract
We resolve difficulties in training and sampling from a discrete generative model by learning a smoothed energy function, sampling from the smoothed data manifold with Langevin Markov chain Monte Carlo (MCMC), and projecting back to the true data manifold with one-step denoising. Our Discrete Walk-Jump Sampling formalism combines the contrastive divergence training of an energy-based model and improved sample quality of a score-based model, while simplifying training and sampling by requiring only a single noise level. We evaluate the robustness of our approach on generative modeling of antibody proteins and introduce the distributional conformity score to benchmark protein generative models. By optimizing and sampling from our models for the proposed distributional conformity score, 97-100% of generated samples are successfully expressed and purified and 70% of functional designs show equal or improved binding affinity compared to known functional antibodies on the first attempt in a single round of laboratory experiments. We also report the first demonstration of long-run fast-mixing MCMC chains where diverse antibody protein classes are visited in a single MCMC chain.
Forward citations
Cited by 2 Pith papers
-
Data-Dependent Smoothing for Protein Discovery with Walk-Jump Sampling
Replacing the single global noise scale in Discrete Walk-Jump Sampling with per-sample noise scales estimated by kernel density estimation improves generation quality on toy and antibody protein data.
-
AffinityFlow: Guided Flows for Antibody Affinity Maturation
AffinityFlow guides AlphaFlow structure generation toward low Rosetta binding energy, then inverse-folds the structures to propose antibody mutations, and reports top scores on a computational affinity maturation benchmark.
Discussion (0). Continue with ORCID to comment.