Posttranslational modifications regulate the location, interactions, and destruction of a protein, controlling fundamental cellular processes. However, unravelling precise effects of these modifications on proteins is challenging because of difficulties obtaining proteins bearing site-specific modifications for structural and functional studies. Furthermore, effects of posttranslational modifications on protein structure are seldom investigated, leaving a gap in our knowledge of how posttranslational modifications modulate protein function. In this presentation, I will discuss our work towards an understanding of the structural effects of posttranslational modifications in instrinsically disordered proteins. I will demonstrate how solid phase peptide synthesis provides access to modified peptides for structural studies and how protein semi-synthesis tools can be used to generate site-specifically modified and segmentally isotope labelled proteins for NMR spectroscopyI aim to show how integrating chemical protein synthesis with structural biology allows us to gain new insights into the effects of protein posttranslational modifications on protein structure, dynamics and regulation.