Abstract
In this paper we investigate the structural and dynamical properties of the two majorporins (OmpF and OmpC) in Escherichia coli, using molecular dynamics (MD)simulations. In particular we characterized the atomic fluctuations, correlatedmotions, temperature dependence, solvent-accessible cross-sectional area and waterdynamics in the key regions of the two channels. Our in-depth analysis allows usto highlight the importance of both the key conserved and substituted residuesbetween OmpF and OmpC. The latter is characterized by a narrower and longerconstriction region with respect to OmpF. OmpC also showed a higher stability uponincreasing temperature. We then present the results of transport properties by usingaccelerated MD simulations to probe the diffusion of norfloxacin (a fluoroquinoloneantibiotic) through the two porins OmpF/OmpC. Our study constitutes a stepforward towards understanding the structure–function relationship of the twoporins’ channels. This will benefit the research of antibacterials with improvedpermeation properties and nanopores that aim to use these porins as sensing systems.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
