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Fast Uncovering of Protein Sequence Diversity from Structure

Luca Alessandro Silva, Barthélémy Meynard-Piganeau, Carlo Lucibello, Christoph Feinauer

2025Year
1Top-tier citations

Abstract

We present InvMSAFold, an inverse folding method for generating protein sequences that is optimized for diversity and speed. For a given structure, InvM-SAFold generates the parameters of a probability distribution over the space of sequences with pairwise interactions, capturing the amino acid covariances observed in Multiple Sequence Alignments (MSA) of homologous proteins. This allows for the efficient generation of highly diverse protein sequences while preserving structural and functional integrity. We show that this increased diversity in sampled sequences translates into greater variability in biochemical properties, highlighting the exciting potential of our method for applications such as protein design. The orders of magnitude improvement in sampling speed compared to existing methods unlocks new possibilities for high-throughput virtual screening.

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