A solid‐state and solution analysis of the homo‐oligopeptides from ε‐tert.‐butyloxycarbonyl‐L‐lysine withp‐oxymethylbenzylcholestan‐3β‐yl succinate asC‐terminal group, using infrared absorption and circular dichroism, is described. The occurrence of intermolecular β‐structure is seen in the solid state and in solvents of low polarity, e.g. methylene chloride, for peptides of intermediate size (from pentamer to decamer). Conversely, the eicosapeptide exhibits a high percentage of α‐helical structure both in the solid state and in 2, 2, 2‐trifluoroethanol. The influence of theC‐terminal group on the conformational preferences of the ε‐blocked homo‐oligolysines in the solid state and in