Protein conformational exchanges modulated by the environment of outer membrane vesicles

29 August 2022, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Protein function, in many cases, is highly related to its frustration status and hence intimately coupled to the dynamics and conformational equilibria of the protein. The environment surrounding proteins is critical for their dynamics and can dra-matically affect the conformational equilibria and subsequently activities of proteins. However, it is yet unclear how protein conformational equilibria are modulated by their crowded native environments. Here we revealed the immunity protein Im7 was less frustrated and shifted toward its ground state in OMVs than in the aqueous solution. Further experiments showed both macromolecular crowding and quinary interactions with the periplasmic components stabilized the ground state of Im7. Our studies highlight the key role of the OMVs environment played on protein conformational equilibria and subsequently conformation-related protein functions. Furthermore, the long-lasting NMR measurement time of proteins within OMVs underlies it could serve as a promising system to investigate protein structures and dynamics in situ via nuclear magnetic spectroscopy.


Protein Excited States
Relaxation Dispersion NMR
Frustrations in Proteins

Supplementary materials

Methods and Materials
quantification by ImageJ, HSQC spectra, correlation between |Δω| in different conditions, solvent PRE, 15N CPMG RD profiles, and the plot of difference of ∆𝑅2,𝑒𝑓𝑓


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