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• W2013237538 startingPage "11364" @default.
• W2013237538 abstract "How the primary sequence of a protein encodes conformational preferences that operate early in folding to promote efficient formation of the correct native topology is still poorly understood. To address this issue, we have prepared a set of yeast iso-1-cytochrome c variants that contain polyalanine inserts ranging from 6 to 30 residues in length near the N terminus of the protein. We study the thermodynamics and kinetics of His-heme loop formation in the denatured state at 3 and 6 M guanidine-HCl concentration. We find that polyalanine closely approximates a random coil with excluded volume giving scaling exponents, ν 3 , for equilibrium loop formation of 2.26 ± 0.13 and 1.97 ± 0.04 in 3 and 6 M guanidine-HCl, respectively. The rate of loop breakage initially decreases and then becomes independent of loop size as would be expected for a random coil. Comparison with previously reported data for denatured state His-heme loop formation for iso-1-cytochrome c and Rhodopseudomonas palustris cytochrome c ′, shows that foldable sequences deviate significantly from random coil behavior and that the deviation is fold-dependent." @default.
• W2013237538 created "2016-06-24" @default.
• W2013237538 creator A5033090342 @default.
• W2013237538 creator A5074549149 @default.
• W2013237538 date "2010-06-07" @default.
• W2013237538 modified "2023-09-27" @default.
• W2013237538 title "Denatured states of low-complexity polypeptide sequences differ dramatically from those of foldable sequences" @default.
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• W2013237538 doi "https://doi.org/10.1073/pnas.1004572107" @default.
• W2013237538 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2895107" @default.
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