The secondary structure of ordered peptides in solution usually exhibits helical distortions that are enhanced by the shortness of the backbone chain. These distortions are reflected in the optical proper-ties of amide NH infrared absorption and in the shape of the CD spectra. These effects are exemplified here in a series of short, intramolecularly H-bonded peptides of the general formula F[(alphaMe)Val](r)-T-[(alphaMe)Val](2)NHt-Bu where T = Toac and F = Fmoc, a nitroxide-based alpha-amino acid quencher and a fluorophoric N-alpha protecting group. respectively, where r = 0-3. Their structural features in methanol were determined by a combined approach of time-resolved fluorescence resonance energy transfer measurements and molecular mechanics calculations. They show a rather compact arrangement of the probes around the distorted, 3(10)-helical backbone chain, which accounts for the slow interconversion between conformational substates on the nanosecond time scale.