ArticleEuropean biophysics journal : EBJ2023
Generation of unfolded outer membrane protein ensembles defined by hydrodynamic properties.
Article in European biophysics journal : EBJ, 2023. 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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Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- A paradigm shift: analytical ultracentrifugation as a multi-attribute platform method in targeted protein degradation.European biophysics journal : EBJ · 2025Article
- The molecular basis for hydrodynamic properties of PEGylated human serum albumin.Biophysical journal · 2024Article
- Seeing is believing: Illuminating the Gram-negative outer membrane with molecular dynamics simulations.Current opinion in structural biology · 2024Review
- Sedimentation velocity FDS studies of antibodies in pooled human serum.European biophysics journal : EBJ · 2023Article
- Proceedings of the 25th Analytical Ultracentrifugation Workshops and Symposium.European biophysics journal : EBJ · 2023Article
- Proceedings of the 25th Analytical Ultracentrifugation Workshops and Symposium.European biophysics journal : EBJ · 2023Article
- Comparison of three AUC techniques for the determination of the loading status and capsid titer of AAVs.European biophysics journal : EBJ · 2023Article
- Strong non-ideality effects at low protein concentrations: considerations for elongated proteins.European biophysics journal : EBJ · 2023Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Outer membrane proteins (OMPs) must exist as an unfolded ensemble while interacting with a chaperone network in the periplasm of Gram-negative bacteria. Here, we developed a method to model unfolded OMP (uOMP) conformational ensembles using the experimental properties of two well-studied OMPs. The overall sizes and shapes of the unfolded ensembles in the absence of a denaturant were experimentally defined by measuring the sedimentation coefficient as a function of urea concentration. We used these data to model a full range of unfolded conformations by parameterizing a targeted coarse-grained simulation protocol. The ensemble members were further refined by short molecular dynamics simulations to reflect proper torsion angles. The final conformational ensembles have polymer properties different from unfolded soluble and intrinsically disordered proteins and reveal inherent differences in the unfolded states that necessitate further investigation. Building these uOMP ensembles advances the understanding of OMP biogenesis and provides essential information for interpreting structures of uOMP-chaperone complexes.
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