title: Describing sequence-ensemble relationships for intrinsically disordered proteins.
abstract: Intrinsically disordered proteins participate in important protein-protein and protein-nucleic acid interactions and control cellular phenotypes through their prominence as dynamic organizers of transcriptional, post-transcriptional and signalling networks. These proteins challenge the tenets of the structure-function paradigm and their functional mechanisms remain a mystery given that they fail to fold autonomously into specific structures. Solving this mystery requires a first principles understanding of the quantitative relationships between information encoded in the sequences of disordered proteins and the ensemble of conformations they sample. Advances in quantifying sequence-ensemble relationships have been facilitated through a four-way synergy between bioinformatics, biophysical experiments, computer simulations and polymer physics theories. In the present review we evaluate these advances and the resultant insights that allow us to develop a concise quantitative framework for describing the sequence-ensemble relationships of intrinsically disordered proteins.
authors.affiliation: Medical Scientist Training Program, Washington University in St. Louis, One Brookings Drive, Campus Box 1097, St. Louis, MO 63130, USA.
authors.forename: Albert H
authors.initials: AH
authors.lastname: Mao
authors.forename: Nicholas
authors.initials: N
authors.lastname: Lyle
authors.forename: Rohit V
authors.initials: RV
authors.lastname: Pappu
mesh_terms: D001665:Binding Sites; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D010455:Peptides; D011506:Proteins; D012997:Solvents; C097188:polyglutamine