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Effects of turn residues in directing the formation of the ß-sheet and in the stability of the ß-sheet

Institute of Chemistry, Academia Sinica, Taipei, Taiwan, R.O.C.

Reprint requests to: Prof. Sunney I. Chan, Institute of Chemistry, Academia Sinica, Taipei, 11529, Taiwan, R.O.C.; e-mail: chans{at}chem.sinica.edu.tw ; fax: 886–2–2783–1237.

The designed peptide (denoted 20-mer, sequence VFITS^DPGKTYTEV^DPGOKILQ) has been shown to form a three-strand antiparallel ß-sheet. It is generally believed that the ^DPro-Gly segment has the propensity to adopt a type II' ß-turn, thereby promoting the formation of this ß-sheet. Here, we replaced ^DPro-Gly with Asp-Gly, which should favor a type I' turn, to examine the influence of different type of turns on the stability of the ß-sheet. Contrary to our expectation, the mutant peptide, denoted P6D, forms a five-residue type I turn plus a ß-bulge between the first two strands due to a one amino-acid frameshift in the hydrogen bonding network and side-chain inversion of the first ß-strand. In contrast, the same kind of substitution at ^DPro-14 in the double mutant, denoted P6DP14D, does not yield the same effect. These observations suggest that the SDGK sequence disfavors the type I' conformation while the VDGO sequence favors a type I' turn, and that the frameshift in the first strand provides a way for the peptide to accommodate a disfavored turn sequence by protruding a bulge in the formation of the ß-hairpin. Thus, different types of turns can affect the stability of a ß-structure.

Keywords: Protein folding; ß-hairpin; ß-sheet; turn; peptide; site-directed mutagenesis; NMR; structure; stability

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