Folding of a miniprotein with mixed fold |
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Authors: | Mohanty Sandipan Hansmann U H E |
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Institution: | John von Neumann Institut für Computing, Forschungszentrum Jülich, Jülich D-52425, Germany. s.mohanty@fz-juelich.de |
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Abstract: | Using the 28 residue betabetaalpha 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 alpha helices and increased formation of beta 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 beta hairpin and forms first. The hydrophobic groups of the helix provide a template which promotes the formation of the beta hairpin that is never observed to form without the helix. |
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