ArticleJournal of molecular biology2007
Sequence composition effects on denatured state loop formation in iso-1-cytochrome c variants: polyalanine versus polyglycine inserts.
Article in Journal of molecular biology, 2007. 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, 15 citations in OpenAlex.
- Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Biochemistry · 2017Article
- Tuning the Flexibility of Glycine-Serine Linkers To Allow Rational Design of Multidomain Proteins.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
- Manifestations of native topology in the denatured state ensemble of Rhodopseudomonas palustris cytochrome c'.Biochemistry · 2011Article
- 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
- Denatured states of low-complexity polypeptide sequences differ dramatically from those of foldable sequences.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Thermodynamics of loop formation in the denatured state of rhodopseudomonas palustris cytochrome c': scaling exponents and the reconciliation problem.Journal of molecular biology · 2009Article
- Importance of contact persistence in denatured state loop formation: kinetic insights into sequence effects on nucleation early in folding.Journal of molecular biology · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein folding is dependent on the formation and persistence of simple loops during the earliest events of the folding process. Ease of loop formation and persistence is believed to be dependent on the steric properties of the residues involved in loop formation. We have investigated this conformational factor in the denatured state of iso-1-cytchrome c using a five alanine insert in front of a unique histidine in the N-terminal region of the protein. The alanine residues have then been progressively substituted with sterically less-constrained glycine residues. Guanidine-HCl unfolding shows that all variants have a free energy of unfolding of approximately 2 kcal/mol. The low stability of these variants is well accounted for by stabilization of the denatured state by histidine-heme loop formation. The stability of the 22 residue histidine-heme loop has been measured in 3 M guanidine hydrochloride for all variants. Surprisingly, relative to alanine, glycine has only a very modest effect on equilibrium loop stability. Thus, the greater flexibility that glycine confers on the main-chain provides no advantage in terms of the persistence of simple loops early in folding. The underlying basis for the similar behavior of loops with polyalanine versus polyglycine inserts is discussed in terms of the current knowledge of the structure and loop formation kinetics of glycine versus alanine-rich peptides.
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