Our molecular dynamics simulations of a distal hairpin from the src SH3 domain in explicit water demonstrate that the folding of a beta-hairpin from the unfolded conformation can occur on an accessible time-scale and the AMBER C96 force field is appropriate for studying beta-hairpin folding. The present study reinforces the experimental results that a proper turn conformation of the distal hairpin that is determined by the tertiary interactions is important for the folding of this hairpin to the native structure. Insight into the folding mechanism of beta-hairpins is obtained from an analysis of the trajectories.