N-substituted glycines oligomers or peptoids have drawn considerable interest as peptide biomimetics [1]. They possess many desirable attributes such as in vivo stability, ease of synthesis, and side chain diversity. Peptoids are also a special class of foldamers, as both cis- and trans-amide bond conformations are accessible. In this respect, peptoids show similarities to proline-rich sequences. For example, they can adopt type I (PPI) and type II (PPII) helical conformations. This involves regulating amide isomerism in the peptoid backbone. Considerable efforts have been made to control the conformation of peptoids through steric and electronic interactions involving peptoid amides and nearby side chains. Among the best cis-amide inducing side chains are the N-chiral aromatic phenylethyl, naphthylethyl and triazolium groups, or the alkyl-ammonium, fluorinated and tert-butyl side chains (Figure 1A). Fewer side chains are capable of promoting trans peptoid amides. Among these, are the N-aryl, N-hydroxy, N-alcoxy, N-acylhydrazide, N-imino and N-alkylamino groups (Fig. 1B). All these findings are recapitulated in a recent review by Kalita et al. [2]. Here we report on our results with the following two sterically demanding aliphatic side chains, tert-butyl (tBu) and (S)-1-tert-butyl(ethyl) (s1tbe), which our group has introduced to the peptoid “tool box” to induce cis-amides. In particular, the modulation of peptoid helicity by sequence specific positioning of chiral (Ns1tbe) and achiral monomers (NtBu) will be discussed [3,4]. We will also consider the conformation of homologous -peptoid oligomers bearing NtBu side chains.