ArticleBiochemistry2008
Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: lessons from the transmembrane protein OmpA.
Article in Biochemistry, 2008. 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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Who cites it
28 citing papers in PubMed, 47 citations in OpenAlex.
- TseCurrent research in microbial sciences · 2026Article
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Genome-wide identification of the opsin protein inFrontiers in microbiology · 2023Article
- The Thermodynamic Stability of Membrane Proteins in Micelles and Lipid Bilayers Investigated with the Ferrichrom Receptor FhuA.The Journal of membrane biology · 2022Article
- Article
- The Uniqueness of Tryptophan in Biology: Properties, Metabolism, Interactions and Localization in Proteins.International journal of molecular sciences · 2020Review
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- Folding of the β-Barrel Membrane Protein OmpA into Nanodiscs.Biophysical journal · 2020Article
- Article
- Position-Specific contribution of interface tryptophans on membrane protein energetics.Biochimica et biophysica acta. Biomembranes · 2018Article
- Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017Review
- Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific.Biochimica et biophysica acta · 2016Article
- Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy.Biochemistry · 2015Article
- Differential contribution of tryptophans to the folding and stability of the attachment invasion locus transmembrane β-barrel from Yersinia pestis.Scientific reports · 2014Article
- Membrane depth-dependent energetic contribution of the tryptophan side chain to the stability of integral membrane proteins.Biochemistry · 2013Article
- Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Spectroscopic and computational study of melittin, cecropin A, and the hybrid peptide CM15.The journal of physical chemistry. B · 2012Article
- Insights into the structure and assembly of Escherichia coli outer membrane protein A.The FEBS journal · 2012Review
- Förster resonance energy transfer as a probe of membrane protein folding.Biochimica et biophysica acta · 2012Article
- The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel.Biophysical chemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Refolding curves of the integral membrane protein outer membrane protein A (OmpA) were measured to determine the conformational stabilities of this model system for membrane protein folding. Wild-type OmpA exhibits a free energy of unfolding (DeltaG degrees H2O) of 10.5 kcal/mol. Mutants, containing a single tryptophan residue at the native positions 7, 15, 57, 102, or 143, are less stable than wild-type OmpA, with DeltaG degrees H2O values of 6.7, 4.8, 2.4, 4.7, and 2.8 kcal/mol, respectively. The trend observed here is discussed in terms of noncovalent interactions, including aromatic interactions and hydrogen bonding. The effect of the soluble tail on the conformational stability of the transmembrane domain of OmpA was also investigated via truncated single-Trp mutants; DeltaG degrees H2O values for four of the five truncated mutants are greater by >2.7 kcal/mol relative to the full-length versions, suggesting that the absence of the soluble domain may destabilize the unfolded transmembrane domain. Finally, dynamic light scattering experiments were performed to measure the effects of urea and protein on vesicle size and stability. Urea concentrations greater than 1 M cause an increase in vesicle size, and these diameters are unaltered in the presence of protein. These dynamic light scattering results complement the fluorescence studies and illustrate the important effects of vesicle size on protein conformational stability.
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