ArticleProtein engineering, design & selection : PEDS2014
An improved Protein G with higher affinity for human/rabbit IgG Fc domains exploiting a computationally designed polar network.
Article in Protein engineering, design & selection : PEDS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Overcoming the Limitations of Protein A: Evolution of Bacterial Protein-Based and Synthetic Affinity Ligands for High-Performance IgG Purification.International journal of molecular sciences · 2026Review
- Precision Labeling of Native Antibodies with Lock Coupling.Journal of the American Chemical Society · 2026Article
- Engineering of an Fc-specific monovalent protein G for the light-controlled affinity purification of antibodies.Scientific reports · 2025Article
- Neural networks to learn protein sequence-function relationships from deep mutational scanning data.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Inferring Protein Sequence-Function Relationships with Large-Scale Positive-Unlabeled Learning.Cell systems · 2021Article
- Improved CUT&RUN chromatin profiling tools.eLife · 2019Article
- Mobile Affinity Sorbent Chromatography.Analytical chemistry · 2018Article
- Kinetic titration series with biolayer interferometry.PloS one · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Protein G is an IgG binding protein that has been widely exploited for biotechnological purposes. Rosetta protein modeling identified a set of favorable polar mutations in Protein G, at its binding interface with the Fc domain of Immunoglobulin G, that were predicted to increase the stability and tighten the binding relative to native Protein G, with only a minor perturbation of the binding mode seen in the crystal structure. This triple mutant was synthesized and evaluated experimentally. Relative to the native protein G, the mutant showed a 3.5-fold enhancement in display level on the surface of yeast and a 5-fold tighter molar affinity for rabbit and human IgG. We attribute the improved affinity to a network of hydrogen bonds exploiting specific polar groups on human and rabbit Fc. The relative specificity increased as well since there was little affinity enhancement for goat and mouse Fc, while the affinity for rat Fc was poorer by half. This designed Protein G will be useful in biotechnological applications as a recombinant protein, where its improved affinity, display and specificity will increase antibody capture sensitivity and capacity. Furthermore, the display of this protein on the surface of yeast introduces the concept of the use of yeast as an affinity matrix.
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Registered trials
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