Pervasive, conserved secondary structure in highly charged protein regions.

ABSTRACT: Understanding how protein sequences confer function remains a defining challenge in molecular biology. Two approaches have yielded enormous insight yet are often pursued separately: structure-based, where sequence-encoded structures mediate function, and disorder-based, where sequences dictate physicochemical and dynamical properties which determine function in the absence of stable structure. Here we study highly charged protein regions (>40% charged residues), which are routinely presumed to be disordered. Using recent advances in structure prediction and experimental structures, we show that roughly 40% of these regions form well-structured helices. Features often used to predict disorder-high charge density, low hydrophobicity, low sequence complexity, and evolutionarily varying length

SUBMITTER: Triandafillou CG 

PROVIDER: S-EPMC9949069 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature