Scaling properties of glycine-rich sequences in guanidine hydrochloride solutions

Michaela L. Finnegan, Bruce E. Bowler

Research output: Contribution to journalArticlepeer-review

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, ν 3, 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 ν 3 = 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, C n, for alanine-rich versus glycine-rich sequences. In 3.0 M GdnHCl, C n(Ala)/C n(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.

Original languageEnglish
Pages (from-to)1969-1978
Number of pages10
JournalBiophysical Journal
Volume102
Issue number8
DOIs
StatePublished - Apr 18 2012

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