## 1 Introduction
### Membrane Proteins of Gram-Negative Bacterium Species

Table 1: _Cont._ \begin{table}
\begin{tabular}{c c c} \hline \hline
**Species** & **Concluding Analysis** & **Membrane** \\  & **Proteins/Channels/Porins** \\ \hline _Escherichia coli_ & Showed quantification of fluoroquinolone norfloxacin transport/uptake via & OmpF \\  & membrane pore [36]. & \\ \hline _Escherichia coli_ & Showed the process of fluoroquinolone enrofloxacin molecule transport [24]. & OmpF \\ \hline _Escherichia coli_ & Evaluated the uptake of cefepime, ceftazidime, and imipenem [78]. & OmpF \\ \hline _Escherichia coli_ & Showed meropenem interaction with the channel and elaborated the & OmpF \\  & binding activity [79]. & \\ \hline _Escherichia coli_ & Reported translocation of polypeptides through membrane protein [80]. & OmpF \\ \hline _Escherichia coli_ & Reported enrofloxacin’s effective interaction across the channel and effective & \\  & modulation of the affinity site in the existence of magnesium ion [81; 82; 83]. & OmpF \\ \hline _Escherichia coli_ & Reported ampicillin and benzyl-penicillin uptake and the effective mechanism & OmpF \\  & involved in the uptake across the outer membrane [84]. & OmpF \\ \hline _Escherichia coli_ & Described and explained the charged residues role in membrane channel & \\  & constriction implicating, channel conductance, ionic selectivity, and & OmpF \\  & voltage-gating [85]. & \\ \hline _Escherichia coli_ & Reported involvement of electrostatic interactions amongst ions and charge & \\  & distribution in the interior of the channel regulating effective ion permeation & OmpF \\  & and selectivity [32]. & \\ \hline _Escherichia coli_ & Reported different amino acid residues ionization states and evaluated & \\  & self-consistently electric potential distribution within the channel [86]. & OmpF \\ \hline _Escherichia coli_ & Explained particular ampicillin molecule movement within the & \\  & membrane pore [87]. & OmpF \\ \hline _Escherichia coli_ & Demonstrated cation selectivity within membrane porin/protein by & \\  & identifying the impact of alkali-metal ions atomic-radii on the site & OmpF \\  & affinity binding [88]. & \\ \hline _Escherichia coli_ & Described particular interaction stuck between grepafloxacin, ciprofloxacin, & \\  & nalidixic acid, and mooxifloxacin with membrane protein [89]. & OmpF \\ \hline _Escherichia coli_ & Explained active permeation of mozifloxacin across membrane protein and & \\  & showed protein/antibiotic interaction [90]. & OmpF \\ \hline _Escherichia coli_ & The effects of four types of polyamines (spermidine, putrescine, cadaverine, & \\  & and spermine) on membrane protein activity were demonstrated & OmpF \\  & and explained [91]. & \\ \hline _Escherichia coli_ & The functional characteristics of four individual amino acid substitutions and & \\  & the impact of a deletion mutant in constriction loop L3 on specific channels & \\  & were demonstrated and explained [92; 93]. & \\ \hline _Escherichia coli_ & The important role of the constriction loop in regulating the voltage-dependent & \\  & gating of intrinsic membrane proteins was demonstrated and explained [94]. & OmpF \\ \hline _Escherichia coli_ & The interactions between nalidixic acid and mozifloxacin antibiotics with & \\  & bacterial proteins were demonstrated and explained [95]. & \\ \hline _Escherichia coli_ & Demonstrated and explained effective ampicillin translocation across the & \\  & membrane protein. Further illustrated the impact of mutations within pores & OmpF \\  & impacting molecular passage [96]. & \\ \hline _Escherichia coli_ & Demonstrated ion pathways along the channel surface [97]. & OmpF \\ \hline _Escherichia coli_ & Explained the interface of particular (HPA3P and magainin 2) peptides with & \\  & the membrane protein and the impact of electric field on pore and & OmpF \\  & peptide geometry [98]. & \\ \hline \hline \end{tabular}
\end{table} 
Table 1: _Cont._