LAUSR

Intrinsically disordered proteins do not adopt well-defined structures, yet they still play functional roles in many different aspects of biology. Their lack of stable conformations poses new challenges to the quantitative description and understanding of their processes, since they cannot be formulated within the classical terms of structural biology. Polymer physics is emerging as a powerful language to identify, describe, and quantify the molecular determinants of the disordered conformational ensemble. Here, I will review the application of key-concepts of polymer theories to intrinsically disordered proteins, with a particular focus on the role played by residue-residue and residue-solvent interactions in modulating conformational transitions in the disordered structural ensemble.