ArticleProtein science : a publication of the Protein Society2010
Increasing protein stability: importance of DeltaC(p) and the denatured state.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Genomic, Proteomic, and Structural Insights Into the Transition of FtsZ From Thermophiles to Mesophiles Across the Prokaryotic Kingdom.Proteins · 2026Article
- Structural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger.Protein science : a publication of the Protein Society · 2024Article
- Genotypic and Phenotypic Spectrum and Pathogenesis of WNT1 Variants in a Large Cohort of Patients With OI/Osteoporosis.The Journal of clinical endocrinology and metabolism · 2023Article
- Helical Propensity Affects the Conformational Properties of the Denatured State of Cytochrome c'.Biophysical journal · 2018Article
- Article
- Application of conventional molecular dynamics simulation in evaluating the stability of apomyoglobin in urea solution.Scientific reports · 2017Article
- Advanced protein formulations.Protein science : a publication of the Protein Society · 2015Review
- Redistribution of flexibility in stabilizing antibody fragment mutants follows Le Châtelier's principle.PloS one · 2014Article
- Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.Biophysical journal · 2012Article
- Residual structure in unfolded proteins.Current opinion in structural biology · 2012Review
- How do thermophilic proteins and proteomes withstand high temperature?Biophysical journal · 2011Article
- Contribution of hydrophobic interactions to protein stability.Journal of molecular biology · 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
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Increasing the conformational stability of proteins is an important goal for both basic research and industrial applications. In vitro selection has been used successfully to increase protein stability, but more often site-directed mutagenesis is used to optimize the various forces that contribute to protein stability. In previous studies, we showed that improving electrostatic interactions on the protein surface and improving the beta-turn sequences were good general strategies for increasing protein stability, and used them to increase the stability of RNase Sa. By incorporating seven of these mutations in RNase Sa, we increased the stability by 5.3 kcal/mol. Adding one more mutation, D79F, gave a total increase in stability of 7.7 kcal/mol, and a melting temperature 28 degrees C higher than the wild-type enzyme. Surprisingly, the D79F mutation lowers the change in heat capacity for folding, DeltaC(p), by 0.6 kcal/mol/K. This suggests that this mutation stabilizes structure in the denatured state ensemble. We made other mutants that give some insight into the structure present in the denatured state. Finally, the thermodynamics of folding of these stabilized variants of RNase Sa are compared with those observed for proteins from thermophiles.
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