Structural perturbation has been extensively used in protein folding studies because it yields valuable conformational information regarding the folding process. Here we have used N-terminal truncation on a cross-linked variant of the GCN4-p1 leucine zipper, aiming to develop a better understanding of the folding mechanism of the coiled-coil motif. Our results indicate that removing the first heptad repeat in this cross-linked GCN4-p1 coiled coil significantly decreases the folding free energy barrier and results in a maximum folding rate of (2.0 +/- 0.3 micros)(-1), which is approximately 50 times faster than that of the full-length protein. Therefore, these results suggest that a set of native or nativelike tertiary interactions, distributed throughout the entire sequence, collectively stabilize the folding transition state of the GCN4-p1 coiled coil. While stable subdomains or triggering sequences have been shown to be critical to the stability of GCN4 coiled coils, our results suggest that the folding of such a subdomain does not seem to dictate the overall folding kinetics.