ArticleProtein science : a publication of the Protein Society2007
Redesigning protein pKa values.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed.
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- Computational design of enhanced detoxification activity of a zearalenone lactonase fromRSC advances · 2019Article
- Rational and Semirational Protein Design.Methods in molecular biology (Clifton, N.J.) · 2018Review
- Sequence homolog-based molecular engineering for shifting the enzymatic pH optimum.Synthetic and systems biotechnology · 2016Article
- Effect of Calcium Ion Removal, Ionic Strength, and Temperature on the Conformation Change in Calmodulin Protein at Physiological pH.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2014Article
- Protein dielectric constants determined from NMR chemical shift perturbations.Journal of the American Chemical Society · 2013Article
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- A collaborative environment for developing and validating predictive tools for protein biophysical characteristics.Journal of computer-aided molecular design · 2012Article
- Gene cloning, expression, and biochemical characterization of an alkali-tolerant β-mannanase from Humicola insolens Y1.Journal of industrial microbiology & biotechnology · 2012Article
- Calculating pH-dependent free energy of proteins by using Monte Carlo protonation probabilities of ionizable residues.Protein & cell · 2012Article
- pKa modulation of the acid/base catalyst within GH32 and GH68: a role in substrate/inhibitor specificity?PloS one · 2012Article
- Computational approaches for rational design of proteins with novel functionalities.Computational and structural biotechnology journal · 2012Review
- On the development of protein pKa calculation algorithms.Proteins · 2011Article
- On the role of electrostatics in protein-protein interactions.Physical biology · 2011Review
- Calculating pKa values in the cAMP-dependent protein kinase: the effect of conformational change and ligand binding.Protein science : a publication of the Protein Society · 2010Article
- Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change.Biophysical journal · 2010Article
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- Solvent reaction field potential inside an uncharged globular protein: a bridge between implicit and explicit solvent models?The Journal of chemical physics · 2007Article
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Authors and funding
2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The ability to re-engineer enzymatic pH-activity profiles is of importance for industrial applications of enzymes. We theoretically explore the feasibility of re-engineering enzymatic pH-activity profiles by changing active site pK(a) values using point mutations. We calculate the maximum achievable DeltapK(a) values for 141 target titratable groups in seven enzymes by introducing conservative net-charge altering point mutations. We examine the importance of the number of mutations introduced, their distance from the target titratable group, and the characteristics of the target group itself. The results show that multiple mutations at 10A can change pK(a) values up to two units, but that the introduction of a requirement to keep other pK(a) values constant reduces the magnitude of the achievable DeltapK(a). The algorithm presented shows a good correlation with existing experimental data and is available for download and via a web server at http://enzyme.ucd.ie/pKD.
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