The entropic force generated by intrinsically disordered segments tunes protein function.

ABSTRACT: Protein structures are dynamic and can explore a large conformational landscape^1,2. Only some of these structural substates are important for protein function (such as ligand binding, catalysis and regulation)^3-5. How evolution shapes the structural ensemble to optimize a specific function is poorly understood^3,4. One of the constraints on the evolution of proteins is the stability of the folded 'native' state. Despite this, 44% of the human proteome contains intrinsically disordered peptide segments greater than 30 residues in length⁶, the majority of which have no known function^7-9. Here we show that the entropic force produced by an intrinsically disordered carboxy terminus (ID-tail) shifts the conformational ensemble of human UDP-α

SUBMITTER: Keul ND 

PROVIDER: S-EPMC6415545 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature