UV resonance Raman (UVR) spectroscopy was used to examine the solution conformation of poly-L-lysine (PLL) and poly-L-glutamic acid (PGA) in their non-a-helical states. UVR measurements indicate that PLL (at pH = 2) and PGA (at pH = 9) exist mainly in a mixture of polyproline II (PPII) and a novel left-handed 2.5(1)-helical conformation, which is an extended P-strand-like conformation with psi approximate to + 170 degrees and Phi approximate to -130 degrees. Both of these conformations are highly exposed to water. The energies of these conformations are very similar. We see no evidence of any disordered "random coil" states. In addition, we find that a PLL and PGA mixture at neutral pH is -60 % beta-sheet and contains PPII and extended 2.5(1)-helix conformations. The beta-sheet conformation shows little evidence of amide backbone hydrogen bonding to water. We also developed a method to estimate the distribution of psi Ramachandran angles for these conformations, which we used to estimate a psi Ramachandran angle energy landscape. We believe that these are the first experimental studies to give direct information on protein and peptide energy landscapes.