Abstract
Determination of affinities and binding sites involved in protein-ligand interactions is essential for understanding molecular mechanisms in biological systems. We combined singular value decomposition and global analysis of NMR chemical shift perturbations caused by protein-protein interactions to determine the number and location of binding sites on the protein surface and to measure the binding affinities. This review focuses on the details of the quantitative analysis of NMR titration data. As an example, the study on the interactions of the intrinsically disordered AD2 subdomain of the tumor suppressor p53 with the TAZ2 domain of the transcriptional coactivator CBP is described.
