13C-NMR relaxation experiments (T1, T2, T1ρ, and NOE) were performed on selectively enriched residues in two peptides, one hydrophobic staple α-helix-forming peptide GFSKAELAKARAAKRGGY and one β-hairpin-forming peptide RGITVNGKTYGR, in water and in water/trifluoroethanol (TFE). Exchange contributions, Rex, to spin-spin relaxation rates for 13Cα and 13Cβ groups were derived and were ascribed to be mainly due to peptide folding-unfolding. To evaluate the exchange time, τex, from Rex, the chemical shift difference between folded and unfolded states, Δδ, and the populations of these states, pi, were determined from the temperature dependence of 13C chemical shifts. For both peptides, values for τex fell in the 1 μs to 10 μs range. Under conditions where the peptides are most folded (water/TFE, 5°C), τex values for all residues in each respective peptide were essentially the same, supporting the presence of a global folding-unfolding exchange process. Rounded-up average τex values were 4 μs for the helix peptide and 9 μs for the hairpin peptide. This 2-3-fold difference in exchange times between helix and hairpin peptides is consistent with that observed for folding-unfolding of other small peptides.