ArticlebioRxiv : the preprint server for biology2025
Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.
Article in bioRxiv : the preprint server for biology, 2025. 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) reversibly 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 homo-chirality 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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