From 3.6 residues-per-turn α-helices in proteins to 10.5 residues-per-turn double helices in B-DNA, biopolymers adopt a wide range of helical secondary structures. Inspired by the diversity of helices observed in nature, we designed a parameter scan to explore the different helix types accessible with a simple 1b1s model. The θ B parameter most easily changes the number of residues-per-turn in this model and is the focus of the next parameter scan. For this parameter scan we varied the θ B from 100 • to 160 • . Other model parameters include: The annealing schedule used for the backbone bond angle parameter scan used the following annealing parameters: T i = 50 B , r a = 0.925, annealing was run for M = 68 cycles, and MC simulations at each temperature are run for N = 10000 steps. Each parameter set was repeated with 100 replicas, to identify a consensus minimum energy structure. Individual simulation replicas for the backbone bond angle, θ B , parameter scan took 38 ± 9 minutes to finish on single core processes. Minimum energy clusters were identified to have sampled from on an average of 52 out of 100 simulations, indicating excellent sampling, with the lowest parameter set sampling 3 out of 100 simulations, again indicating a significant level of repeatability when using a large number of replicas. Findings from this experiment are described in the results and discussion in section 3.3.