ArticleBiochimica et biophysica acta. Biomembranes2018
Position-Specific contribution of interface tryptophans on membrane protein energetics.
Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 12 citations in OpenAlex.
- Roles of inter- and intramolecular tryptophan interactions in membrane-active proteins revealed by racemic protein crystallography.Communications chemistry · 2023Article
- The Thermodynamic Stability of Membrane Proteins in Micelles and Lipid Bilayers Investigated with the Ferrichrom Receptor FhuA.The Journal of membrane biology · 2022Article
- Engineering a HyperstableJournal of the American Chemical Society · 2022Article
- The Role of Extracellular Loops in the Folding of Outer Membrane Protein X (OmpX) ofFrontiers in molecular biosciences · 2022Article
- Reversible folding energetics of Yersinia Ail barrel reveals a hyperfluorescent intermediate.Biochimica et biophysica acta. Biomembranes · 2020Article
- Tryptophan usage by Helicobacter pylori differs among strains.Scientific reports · 2019Article
- Hydrophobic Mismatch Modulates Stability and Plasticity of Human Mitochondrial VDAC2.Biophysical journal · 2018Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Interface tryptophans are key residues that facilitate the folding and stability of membrane proteins. Escherichia coli OmpX possesses two unique interface tryptophans, namely Trp76, which is present at the interface and is solvent-exposed, and Trp140, which is relatively more lipid solvated than Trp76 in symmetric lipid membranes. Here, we address the requirement for tryptophan and the consequences of aromatic amino acid substitutions on the folding and stability of OmpX. Using spectroscopic measurements of OmpX-Trp/Tyr/Phe mutants, we show that the specific mutation W76→Y allows barrel assembly >1.5-fold faster than native OmpX, and increases stability by ~0.4kcalmol
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