ArticleProceedings of the National Academy of Sciences of the United States of America2010
Denatured states of low-complexity polypeptide sequences differ dramatically from those of foldable sequences.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Denatured State Conformational Biases in Three-Helix Bundles Containing Divergent Sequences Localize near Turns and Helix Capping Residues.Biochemistry · 2021Article
- Helical Propensity Affects the Conformational Properties of the Denatured State of Cytochrome c'.Biophysical journal · 2018Article
- Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Biochemistry · 2017Article
- Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions.Biophysical journal · 2012Article
- Tryptophan stabilizes His-heme loops in the denatured state only when it is near a loop end.Biochemistry · 2012Article
- Scaling properties of glycine-rich sequences in guanidine hydrochloride solutions.Biophysical journal · 2012Article
- Residual structure in unfolded proteins.Current opinion in structural biology · 2012Review
- Manifestations of native topology in the denatured state ensemble of Rhodopseudomonas palustris cytochrome c'.Biochemistry · 2011Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
- Propensities of aromatic amino acids versus leucine and proline to induce residual structure in the denatured-state ensemble of iso-1-cytochrome c.Journal of molecular biology · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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, nu(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.
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