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- W2065359898 abstract "Although much has been learned about the design of models of β-sheets during the last decade, modest fold stabilities in water and terminal fraying remain a feature of most β-hairpin peptides. In the case of hairpin capping, nature did not provide guidance for solving the problem. Some observations from prior turn capping designs, with further optimization, have provided a generally applicable, “unnatural” beta cap motif (alkanoyl-Trp at the N terminus and Trp-Thr-Gly at the C terminus) that provides a net contribution of 6 + kJ/mol to β-hairpin stability, surpassing all other interactions that stabilize β-hairpins including the covalent disulfide bond. The motif, made up entirely of natural residues, is specific to the termini of antiparallel β-strands and reduces fraying at the ends of hairpins and other β-sheet models. Utilizing this motif, 10- to 22-residue peptide scaffolds of defined stereochemistry that are greater than 98% folded in water have been prepared. The β-cap can also be used to staple together short antiparallel β-strands connected by a long flexible loop." @default.
- W2065359898 created "2016-06-24" @default.
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- W2065359898 date "2010-05-19" @default.
- W2065359898 modified "2023-09-23" @default.
- W2065359898 title "Stabilizing capping motif for β-hairpins and sheets" @default.
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- W2065359898 doi "https://doi.org/10.1073/pnas.0913534107" @default.
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