Folding is a fundamental physical phenomenon by which peptides and proteins fold into their characteristic three-dimensional compact structures – almost always mediated by a myriad of non-covalent forces. Understanding the folding pattern of peptides and proteins is vital to the understanding of their 3-dimensional structure and function. Owing to their sheer size and intricacy, proteins pose considerable challenges in investigating and understanding their folding patterns. Thus, the first step towards unravelling the mysteries behind protein folding is to understand closely how it's smaller counterpart - a peptide folds. Over the years, we have been carrying out conformational mapping of synthetic oligomers of well defined size. Our extensive efforts have culminated in the development of diverse classes of synthetic ologomers with intriguing folding propensities and potential for utility in biomedical science – particularly for the structural rigidification of bioactive peptides. The discovery of the Ant-Pro reverse turn is clearly noteworthy, in this regard.