ArticleStructure (London, England : 1993)2014
Random single amino acid deletion sampling unveils structural tolerance and the benefits of helical registry shift on GFP folding and structure.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 70 citations in OpenAlex.
- Exploring the deletion landscape ofbioRxiv : the preprint server for biology · 2025Article
- Deep indel mutagenesis reveals the impact of amino acid insertions and deletions on protein stability and function.Nature communications · 2025Article
- Middle East respiratory syndrome coronavirus (MERS-CoV) internalization does not rely on DPP4 cytoplasmic tail signaling.Npj viruses · 2024Article
- Structural and energetic analysis of stabilizing indel mutations.bioRxiv : the preprint server for biology · 2024Article
- Insertion-Deletion Events Are Depleted in Protein Regions with Predicted Secondary Structure.Genome biology and evolution · 2024Article
- Computational modeling and prediction of deletion mutants.Structure (London, England : 1993) · 2023Article
- DIMPLE: deep insertion, deletion, and missense mutation libraries for exploring protein variation in evolution, disease, and biology.Genome biology · 2023Article
- A review of visualisations of protein fold networks and their relationship with sequence and function.Biological reviews of the Cambridge Philosophical Society · 2023Review
- An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleation.Nature communications · 2022Article
- Comparative Genomics of Six LyticPHAGE (New Rochelle, N.Y.) · 2022Article
- Using the Evolutionary History of Proteins to Engineer Insertion-Deletion Mutants from Robust, Ancestral Templates Using Graphical Representation of Ancestral Sequence Predictions (GRASP).Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Comprehensive deletion landscape of CRISPR-Cas9 identifies minimal RNA-guided DNA-binding modules.Nature communications · 2021Article
- A novel framework for engineering protein loops exploring length and compositional variation.Scientific reports · 2021Article
- Structure-guided engineering of adenine base editor with minimized RNA off-targeting activity.Nature communications · 2021Article
- mGreenLantern: a bright monomeric fluorescent protein with rapid expression and cell filling properties for neuronal imaging.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Folliculin variants linked to Birt-Hogg-Dubé syndrome are targeted for proteasomal degradation.PLoS genetics · 2020Article
- Accessing unexplored regions of sequence space in directed enzyme evolution via insertion/deletion mutagenesis.Nature communications · 2020Article
- Tubulin-Dependent Transport of Connexin-36 Potentiates the Size and Strength of Electrical Synapses.Cells · 2019Article
- Fitness Effects of Single Amino Acid Insertions and Deletions in TEM-1 β-Lactamase.Journal of molecular biology · 2019Article
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5 authors at 1 institution in 1 country.
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Abstract
Altering a protein's backbone through amino acid deletion is a common evolutionary mutational mechanism, but is generally ignored during protein engineering primarily because its effect on the folding-structure-function relationship is difficult to predict. Using directed evolution, enhanced green fluorescent protein (EGFP) was observed to tolerate residue deletion across the breadth of the protein, particularly within short and long loops, helical elements, and at the termini of strands. A variant with G4 removed from a helix (EGFP(G4Δ)) conferred significantly higher cellular fluorescence. Folding analysis revealed that EGFP(G4Δ) retained more structure upon unfolding and refolded with almost 100% efficiency but at the expense of thermodynamic stability. The EGFP(G4Δ) structure revealed that G4 deletion caused a beneficial helical registry shift resulting in a new polar interaction network, which potentially stabilizes a cis proline peptide bond and links secondary structure elements. Thus, deletion mutations and registry shifts can enhance proteins through structural rearrangements not possible by substitution mutations alone.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.