Abstract
NMR spectroscopy has been established as a potent method for the detn. of foldamer structures in soln. However, the NMR techniques could be limited by averaging, so addnl. exptl. techniques are often needed to fully endorse the folding properties of a sequence. The authors have recently demonstrated that oligo-γ-peptides composed of 4-amino(methyl)-1,3-thiazole-5-carboxylic acids (ATCs) adopt an original helical fold stabilized by hydrogen bonds forming C9 pseudocycles. The main objective of the present work is to restudy the folding of ATC oligomer 1 to identify reliable FTIR and NMR structural markers that are of value for tracking the degree of organization of ATC-based peptides.