Helices are the most common structural pattern observed in structured proteins. Polypeptide sequences that form helices in isolation have been identified and extensively studied. These are generally rich in alanine, the amino acid with strongest helical propensity. Insertion of charged or polar amino acids has been shown to be necessary to make alanine-rich peptides soluble and sometimes even increase the helicity of the peptides. More recently sequences that contain mostly charged residues (E-R/K rich) have been found in naturally occurring proteins that are highly helical, soluble, and extended regardless their length. Artificial sequences composed mostly or exclusively of charged amino acids have been designed that are also highly helical, depending on the specific pattern of oppositely charged residues. Here we explore the thermodynamic properties of a number of 16-residue long peptides with varying helical propensity by performing equilibrium simulations over a broad range of temperatures. We observe quantitative differences in the peptides' helical propensities that can be related to qualitative differences in the free energy landscape, depending on the ampholytic patterns in the sequence. The results provide hints on how the specific physical properties of naturally occurring long sequences with similar patterns of charged residues may relate to their biological function.