We have investigated the folding pathway of the 36‐residue villin headpiece subdomain (HP‐36) by action‐derived molecular dynamics simulations. The folding is initiated by hydrophobic collapse, after which the concurrent formation of full tertiary structure and α‐helical secondary structure is observed. The collapse is observed to be associated with a couple of specific native contacts contrary to the conventional nonspecific hydrophobic collapse model. Stable secondary structure formation after the collapse suggests that the folding of HP‐36 follows neither the framework model nor the diffusion‐collision model. The C‐terminal helix forms first, followed by the N‐terminal helix positioned in its native orientation. The short middle helix is shown to form last. Signs for multiple folding pathways are also observed. © 2009 Wiley Periodicals, Inc. J Comput Chem 2010