ArticleProtein science : a publication of the Protein Society2005
Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Denatured State Conformational Biases in Three-Helix Bundles Containing Divergent Sequences Localize near Turns and Helix Capping Residues.Biochemistry · 2021Article
- Ion-ion interactions in the denatured state contribute to the stabilization of CutA1 proteins.Scientific reports · 2018Article
- Microbial ribonucleases (RNases): production and application potential.World journal of microbiology & biotechnology · 2015Review
- Energetically significant networks of coupled interactions within an unfolded protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Increased alkalotolerant and thermostable ribonuclease (RNase) production from alkaliphilic Streptomyces sp. M49-1 by optimizing the growth conditions using response surface methodology.World journal of microbiology & biotechnology · 2013Article
- Rational modification of protein stability by targeting surface sites leads to complicated results.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- 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
- Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins.Protein science : a publication of the Protein Society · 2010Article
- Effective approach for calculations of absolute stability of proteins using focused dielectric constants.Proteins · 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
- Thermally denatured state determines refolding in lipase: mutational analysis.Protein science : a publication of the Protein Society · 2009Article
- Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Characterization of the unfolded state of repeat proteins.HFSP journal · 2008Article
- Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa.Biophysical journal · 2008Article
- Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability.Archives of biochemistry and biophysics · 2008Article
- Increasing protein conformational stability by optimizing beta-turn sequence.Journal of molecular biology · 2007Article
- Sequence composition effects on denatured state loop formation in iso-1-cytochrome c variants: polyalanine versus polyglycine inserts.Journal of molecular biology · 2007Article
- Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions.Biophysical journal · 2006Article
- Native state energetics of the Src SH2 domain: evidence for a partially structured state in the denatured ensemble.Protein science : a publication of the Protein Society · 2006Article
- pK values of the ionizable groups of proteins.Protein science : a publication of the Protein Society · 2006Article
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4 authors.
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Abstract
Gaining a better understanding of the denatured state ensemble of proteins is important for understanding protein stability and the mechanism of protein folding. We studied the folding kinetics of ribonuclease Sa (RNase Sa) and a charge-reversal variant (D17R). The refolding kinetics are similar, but the unfolding rate constant is 10-fold greater for the variant. This suggests that charge-charge interactions in the denatured state and the transition state ensembles are more favorable in the variant than in RNase Sa, and shows that charge-charge interactions can influence the kinetics and mechanism of protein folding.
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