## 1 Introduction
### Membrane Proteins of Gram-Negative Bacterium Species
\begin{table}
\begin{tabular}{c c c} \hline \hline
**Species** & **Concluding Analysis** & **Membrane** \\  & **Proteins/Channels/Porins** \\ \hline _Escherichia coli_ & Reported a particular mechanism of translocation of ampicillin via membrane protein [99]. & OmpF \\ \hline _Escherichia coli_ & Reported particular interaction/binding of carbenicillin, and ampicillin & OmpF \\  & & etrapenem, within the membrane protein [100]. & OmpF \\ \hline _Escherichia coli_ & Explained specific interactions engaged in the transport/translocation of amoxicillin, ampicillin, azlocillin, carbenicillin, and piperacillin [44]. & OmpF \\ \hline _Escherichia coli_ & Explained the influence of particular acid residue (D113A) substitution on ceftazidine, cefotaxime, cefiprome, cefepime, cefoxitin, and ampicillin & OmpF \\  & bacterial susceptibility [101]. & OmpF \\ \hline _Escherichia coli_ & Reported the operational anti-loop 3 residue (Lys-16) position in cefepime transport across membrane protein [102]. & OmpF \\ \hline _Escherichia coli_ & Explained ionic concentration and charged residues in membrane protein & OmpC \\  & present at constriction zone and their impact over intrinsic gating behavior of membrane protein [103]. & OmpC \\ \hline _Escherichia coli_ & Explained trio mutations in the interior of isolated porins from multi-drug resistant bacterium. Further, demonstrated the resulting mutations affecting the transport of cefotaxime [104]. & OmpC \\ \hline _Escherichia coli_ & Demonstrated and explained effective interaction of ceftaxone, cefiprome, and ceftazidine with membrane protein [105]. & OmpC, OmpF \\ \hline _Escherichia coli_ & Reported an effective influx of cefepime, enrofloxacin, norfloxacin, ciprofloxacin, ceftazidine, and ceftaxone [106]. & OmpC, OmpF \\ \hline _Escherichia coli_ & Demonstrated the impact of culture medium over effective membrane protein expression and showed the effect on taxobactam-piperacillin susceptibility [107]. & OmpC, OmpF \\ \hline _Escherichia coli_ & Demonstrated by exploiting water as an analytical tool, a distinctive macroscopic electric field within water-filled channels [108]. & OmpF, OmpC \\ \hline _Escherichia coli_ & The successful penetration of meropenem and imipenem was demonstrated and explained. It was also shown that their uptake relies on the alignment of the molecule’s electric dipole with the membrane protein’s interior electric field. Moreover, certain regions within the membrane protein were identified as preorientation sites that affect the pathway of the molecules [109]. & OmpF, OmpC \\ \hline _Escherichia coli_ & Demonstrated and explained excess of positively charged fixed ions within the interior of the membrane protein. As a result, the protein exhibits a characteristic selectivity towards anions [110]. & PhoE \\ \hline _Escherichia coli_ & The influence of lysine and carboxyl groups on the inherent ionic selectivity of the membrane pore was demonstrated and explained [111]. & PhoE \\ \hline _Enterobacter_ & & (Omp35, Omp36), \\ _aerogenes,_ & Demonstrated and explained the transport of different antibiotic & (Omp535, Omp536), \\ _Enterobacter cloaceae_ & membrane proteins [23]. & (OmpK35 OmpK36) \\ _Klebsiella pneumoniae_ & Demonstrated possible system of antibiotic resistance by mutational loss of membrane proteins. Further, effectively demonstrated quantitative influx rates for different antibiotics such as erythromycin, novobiocin, colacacillin, benzylpenicillin, ampicillin, cephaloridine, cefoxitin, cephalothin, ceftazidine, cefepime, cefotaxime, cefamandole, imipenem, ceftriaxone and etrapenem [112]. & Omp35, Omp36 \\ \hline _Enterobacter_ & & OmpK35, OmpK36 \\ _aero-genesE. Aerogenes, Klebsiella pneumoniae, Wikimedia coli_ & Demonstrated outer membrane porins role over avibactam-ceftazidine diffusion via outer membrane [113]. & OmpF, OmpC \\ \hline \hline \end{tabular}
\end{table} 
Table 1: Cont. \begin{table}
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