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Versatility from Protein Disorder

The notion that dis ordered regions are largely passive is being actively challenged by the idea that they perform diverse functions, and that synergy between structured and disordered regions expands the functional repertoires of proteins.

Sequence complexity of disordered protein

The Swiss Protein database of sequences exhibits significantly higher amounts of both low‐complexity and predicted‐to‐be‐disordered segments as compared to a non‐redundant set of sequences from the Protein Data Bank, providing additional data that nature is richer in disordered and low-complexity segments compared to the commonness of these features in the set of structurally characterized proteins.