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Generation of Unfolded Outer Membrane Protein Ensembles Targeted by Hydrodynamic Properties

Devlin, T.; Fleming, P. J.; Loza, N.; Fleming, K. G.

2022-11-01 biophysics
10.1101/2022.10.31.514552 bioRxiv
Show 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 experimental properties of two well-studied OMPs. The overall size and shape of the unfolded ensembles in water 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 reveal inherent differences in the unfolded states that necessitate further investigation. Building these uOMP ensembles advances the understanding of OMP biogenesis and produces essential information for interpreting structures of uOMP-chaperone complexes.

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