Chen P.-Y.CHIH-KAI LINLee C.-T.Jan H.Chan S.I.2022-10-122022-10-122001https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034854541&doi=10.1110%2fps.49001&partnerID=40&md5=b922634443afa455b32e488edc831bb6https://scholars.lib.ntu.edu.tw/handle/123456789/623504The designed peptide (denoted 20-mer, sequence VFITSDPGKTYTEVDPGOKILQ) has been shown to form a three-strand antiparallel β-sheet. It is generally believed that the DPro-Gly segment has the propensity to adopt a type II′ β-turn, thereby promoting the formation of this β-sheet. Here, we replaced DPro-Gly with Asp-Gly, which should favor a type 1′ turn, to examine the influence of different type of turns on the stability of the β-sheet. Contrary to our expectation, the mutant peptide, denoted P6D, forms a five-residue type I turn plus a β-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 β-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 β-hairpin. Thus, different types of turns can affect the stability of a β-structure.β-hairpin; β-sheet; NMR; Peptide; Protein folding; Site-directed mutagenesis; Stability; Structure; Turn[SDGs]SDG14amino acid; hydrogen; peptide; protein; article; circular dichroism; hydrogen bond; nuclear magnetic resonance; nuclear Overhauser effect; priority journal; protein folding; protein stability; site directed mutagenesis; Amino Acid Sequence; Amino Acid Substitution; Circular Dichroism; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptides; Protein Structure, Secondary; Structure-Activity Relationship; ThermodynamicsEffects of turn residues in directing the formation of the β-sheet and in the stability of the β-sheetjournal article10.1110/ps.490012-s2.0-0034854541