Assessing energetic contributions to binding from a disordered region in a protein-protein interaction .

ABSTRACT: Many functional proteins are at least partially disordered prior to binding. Although the structural transitions upon binding of disordered protein regions can influence the affinity and specificity of protein complexes, their precise energetic contributions to binding are unknown. Here, we use a model protein-protein interaction system in which a locally disordered region has been modified by directed evolution to quantitatively assess the thermodynamic and structural contributions to binding of disorder-to-order transitions. Through X-ray structure determination of the protein binding partners before and after complex formation and isothermal titration calorimetry of the interactions, we observe a correlation between protein ordering and binding affinity for complexes along this affinity

SUBMITTER: Cho S 

PROVIDER: S-EPMC2964404 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature