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• W2017340701 abstract "The intrinsic polymer properties of glycine-rich sequences are evaluated with a set of iso-1-cytochrome c variants with N-terminal inserts of the sequence (GGGGGK)n for n = 1–5. The thermodynamics and kinetics of His-heme loop formation are measured as a function of guanidine hydrochloride (GdnHCl) concentration for loop sizes ranging from 22 to 46 residues. The scaling exponent for loop formation, ν3, evaluated using the Jacobson-Stockmayer equation is near 1.8, at 1.5 and 3.0 M GdnHCl, but it increases to 2.2 in 6.0 M GdnHCl. Previous work on a set of iso-1-cytochrome c variants with (AAAAAK)n inserts gave ν3 = 2.2 for alanine-rich sequences in both 3.0 and 6.0 M GdnHCl. Chain stiffness was evaluated from the relative magnitude of Flory's characteristic ratio, Cn, for alanine-rich versus glycine-rich sequences. In 3.0 M GdnHCl, Cn(Ala)/Cn(Gly) is 1.6, decreasing to 1.3 in 6.0 M GdnHCl. The data suggest that solvent-backbone interactions dominate polypeptide conformational properties under good solvent conditions whereas side-chain-dependent properties are more important under poor solvent conditions. The results provide a direct experimental assessment in terms of polymer properties of the distinct roles of Gly versus Ala in the folding code." @default.
• W2017340701 created "2016-06-24" @default.
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• W2017340701 date "2012-04-01" @default.
• W2017340701 modified "2023-09-26" @default.
• W2017340701 title "Scaling Properties of Glycine-Rich Sequences in Guanidine Hydrochloride Solutions" @default.
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• W2017340701 doi "https://doi.org/10.1016/j.bpj.2012.03.049" @default.
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