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• W1996982068 abstract "αtα is a de novo designed 38-residue peptide [Fezoui et al. (1995) Protein Sci. 4, 286−295] that adopts a helical hairpin conformation in solution [Fezoui et al. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 3675−3679; Fezoui et al. (1997) Protein Sci. 6, 1869−1877]. Since αtα was developed as a model system for protein folding at the stage where secondary structures interact and become mutually stabilizing, it is of interest to investigate the increase in stability that occurs with helix association. αtα was dissected into its component helices and the relative stabilities of the individual helices and the parent molecule were assessed. The ΔG0 of unfolding of αtα measured by guanidine hydrochloride denaturation was determined to be 3.4 kcal/mol. The equilibrium constant for folding of αtα was estimated from the ΔG0 as 338 and from hydrogen exchange measurements as 259. The stability of the helices in intact αtα over the individual helices increased by a factor of at least 37 based on amide proton exchange measurements. Sedimentation equilibrium studies showed very little association of the peptides to form either homo- or heterodimers, suggesting that helix association is stabilized by the high effective concentration of the helices caused by the presence of the connecting turn. The effects of salt and pH on the helicity of the component peptides are largely reflected in the intact molecule, implying that short-range interactions still make important contributions to the conformation of the intact molecule even though significant stabilization is caused by helix association." @default.
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• W1996982068 date "1999-02-11" @default.
• W1996982068 modified "2023-10-16" @default.
• W1996982068 title "Dissection of the de Novo Designed Peptide αtα: Stability and Properties of the Intact Molecule and Its Constituent Helices" @default.
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• W1996982068 doi "https://doi.org/10.1021/bi9823838" @default.
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