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Substantial questions remain about the process of protein folding, including whether transient intermediates exist with significantly different secondary structure than the final fold. The src SH3 domain is a highly beta-rich structure with five betastrands. We report here a far-UV circular dichroism investigation of the refolding of His-tagged Src SH3 at subzero temperatures. We observed a transient a-helix-rich intermediate, indicating that the early stages of protein folding can involve the formation of intermediates with very different structures from the final conformation.

Transient Alpha-helical Structure during Folding of Src SH3 Domain at Subzero Temperatures