Folding of a miniprotein with mixed fold

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Using the 28 residue ßßα protein FSD-EY as a target system, we examine correction terms for the ECEPP/3 force field. We find an increased probability of formation of the native state at low temperatures resulting from a reduced propensity to form α helices and increased formation of ß sheets. Our analysis of the observed folding events suggests that the C -terminal helix of FSD-EY is much more stable than the N -terminal ß hairpin and forms first. The hydrophobic groups of the helix provide a template which promotes the formation of the ß hairpin that is never observed to form without the helix. © 2007 American Institute of Physics.

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Journal of Chemical Physics