| Details: |
Unlike folded proteins, intrinsically disordered proteins (IDPs) lack a well-defined dimensional
structure, challenging the conventional structure–function paradigm. Their sequences typically
contain few hydrophobic residues and an abundance of charged and polar amino acids, making
them analogous to polyampholytes with tunable flexibility. Using the venerable Kremer–Grest
model, we demonstrate that the interplay between charge patterning and bending rigidity dictates
the equilibrium structures of polyampholytes, often giving rise to exotic morphologies.
Furthermore, employing various minimalist models, we investigate the LAF1 sequence and its
shuffled variants, and show that their energy landscapes encode distinctive structural features. |