ArticleProceedings of the National Academy of Sciences of the United States of America2026
Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Many protein low-complexity domains (LCDs) self-associate to enable cellular function, yet fundamental questions remain regarding how polypeptide chemical and structural features beyond side chain identity contribute to LCD-LCD interactions. For instance, the folds adopted by globular proteins emerge from constraints enforced by homochirality of genetically encoded polypeptides. However, it remains unclear to what extent similar geometric constraints apply to LCD self-association. Herein, we use protein total and semi-synthesis to probe the contribution of C
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