A simple method for mapping the location of cross-β-forming regions within protein domains of low sequence complexity

• DOI: 10.1073/pnas.2503382122
• Publication Date: 2025-04-23T17:37:33Z
• Authors: Jinge Gu; Xiaoming Zhou; Lillian Sutherland; Glen Liszczak; Steven L. McKnight
• Keywords: Sequence (biology)

Protein domains of low sequence complexity are unable to fold into stable, three-dimensional structures. In test tube studies, these unusual polypeptide regions can self-associate in a manner causing phase separation from aqueous solution. This form protein:protein interaction has been implicated numerous examples dynamic morphological organization within eukaryotic cells. several cases, the basis for domain (LCD) self-association and traced formation labile cross-β The primary energetic force favoring transient reversible structures is enabled by backbone interactions. Short, contiguous networks peptide amino groups carbonyl oxygens zippered together intermolecularly hydrogen bonding as described Linus Pauling seven decades ago. Here, we describe simple, molecular biological method useful identification localized, self-associating larger protein complexity.