Small proteins provide good model systems for studying the fundamental forces that control protein folding. Here, we investigate the folding dynamics of the 28 residue zinc-finger mutant FSD-1, which is designed to form a metal-independent folded beta beta alpha-motif, and which provides a testing ground for proteins containing a mixed alpha/beta fold. Although the folding of FSD-1 has been actively studied, the folding mechanism remains largely unclear. In particular, it is unclear in what stage of folding the a-helix is formed. To address this issue we investigate the folding mechanism of FSD-1 using a combination of temperature-dependent UV circular dichroism (UV-CD), Fourier transform infrared (FTIR) spectroscopy, two-dimensional infrared (2D-IR) spectroscopy, and temperature jump (T-jump) transient-IR spectroscopy. Our UV-CD and FTIR data show different thermal melting transitions, indicating multistate folding behavior. Temperature-dependent 2D-IR spectra indicate that the a-helix is the most stable structural element of FSD-1. To investigate the folding/unfolding re-equilibration dynamics of FSD-1, the conformational changes induced by a nanosecond T-jump are probed with transient-IR and transient dispersed-pump probe (DPP) IR spectroscopy. We observe biexponential T-jump relaxation kinetics (with time constants of 80 +/- 13 ns and 1300 +/- 100 ns at 322 K), confirming that the folding involves an intermediate state. The IR and dispersed-pump probe IR spectra associated with the two kinetic components suggest that the folding of FSD-1 involves early formation of the alpha-helix, followed by the formation of the beta-hairpin and hydrophobic contacts.