## 3 Results and Discussion
### Interaction between Uunami Dipeptides and Rattus Norvegicus mGluR1 Open-Open Conformation  
Table 3 and Figure 3 are presented hereunder, outlining the interactions in this case. \begin{table}
\begin{tabular}{c c c c c c c c} \hline \hline \multirow{2}{*}{**Legend**} & \multirow{2}{*}{**PubChem**} & \multirow{2}{*}{**Binding Energy**} & \multirow{2}{*}{**Inhibition**} & \multicolumn{2}{c}{**Protein Residues Involved**} & \multicolumn{2}{c}{**Protein Residues Involved in**} & \multicolumn{2}{c}{**Protein Residues**} \\  & & & & **in H-Bond Interactions** & & **Involvested in Salt Bridges** \\  & & & & **Claim-Reside** & & **No. of** & **Hydrophobic Interactions** & **[**Claim-Reside** \\  & & & & **(Distance by Donor-Acceptor)** & & **H-Bonds** & **[**Claim-Reside** & **[**Distance by Contesy of Charge]** \\  & & & & **(Distance by Donor-Acceptor)** & & **(Protein Donor/Acceptor,** & **(Cipton Atomomal)]** & **(Cipton National Group** \\  & & & & **Resident from Stide Chain)** & & **Providing the Charge]** \\ \hline \multirow{2}{*}{E} & \multirow{2}{*}{33,032} & \multirow{2}{*}{\(-\)4.31} & \multirow{2}{*}{694.05} & A:Tyr4 (3.31 A) (Acceptor,sd) & & & A:A:Arg78 (3.91 A) (Acceptor,sd) \\  & & & & A:Tyr4 (2.97 A) (Acceptor,sd) & & & A:Arg49 (3.90 A) (Carbesian) \\  & & & & A:Ser165 (3.00 A) (Chomost,sd) & & & & A:Arg49 (2.49 A) (Carbesian) \\ \hline \multirow{4}{*}{AH} & \multirow{4}{*}{9,837,455} & \multirow{4}{*}{\(-\)6.70} & \multirow{4}{*}{12.32} & A:Ser165 (3.43 A) (Dororor) & & & & \\  & & & & A:Ser165 (3.93 A) (Dororor) & & & & \\  & & & & A:Ser165 (3.93 A) (Dororor) & & & & \\  & & & & A:Tyr4 (3.93 A) (Acceptor,sd) & & & & \\  & & & & A:Ser165 (3.93 A) (Dororor) & & & & \\  & & & & A:Tyr4 (3.93 A) (Dororor,sd) & & & & \\  & & & & & A:Tyr4 (3.93 A) (Dororor,sd) & & & \\ \hline \multirow{2}{*}{DA} & \multirow{2}{*}{5,491,963} & \multirow{2}{*}{\(-\)4.76} & \multirow{2}{*}{322.75} & A:Tyr4 (3.63 A) (Acceptor,sd) & & & & A:Arg71 (3.58 A) (Carbesian) \\  & & & & A:G**G  
\begin{table}
\begin{tabular}{c c c c c c c c} \hline \hline  & & & & & **Protein Residues Involved** & & & **Protein Residues** \\
**Ligand** & **PubChem Chem** & **Binding Energy** & **Inhibition** & **in H-Bond Interactions** & **In hydrophobic Interactions** & **Involide in Salt Bridges** \\
**Ligand** & **ID** & **(kcal/mol)** & **Constant** & **(****Lina-Residucito** & **No. of** & **[Chain-Residucito** & **[Chain-Residucito** \\
**(M)** & & & & **(****Distance bw  
Figure 3: Two-dimensional representation of protein–ligand interactions between _Rattus norregicus_ open–open conformation of mGluR1 (PDB ID: 1 EWT) and Glu (PubChemChem ID: 33032), AH (PubChemChem ID: 9837455), DA (PubChem ID: 5491963), DG (PubChemChem ID: 151148), EE (PubChem ID: 439500), ES (PubChemChem ID: 6995653), EV (PubChem ID: 6992567), VG (PubChem ID: 699311). H bonds are shown as dashed lines, hydrophobic contacts are represented by green splines; the corresponding pocket residues are also shown in the same color. Diagrams obtained from the ProteinsPlus PoseView tool, from which E  
amino acid was predicted to interact with Tyr74, Arg78, Ser186 and Lys409 by H-bonds; AH, with Tyr74, Arg78, Gly163, Ser186 and Lys409 by H-bonds and Ser186 by a hydrophobic interaction; DA, with Arg71 and Lys409 by H-bonds; DG, with Tyr74, Ser186, Lys409 by H-bonds; EE, with Arg71, Arg78, Ser186, Glu292 and Lys409 by H-bonds and Trp110 by hydrophobic interaction; ES, with Tyr74, Asp318 and Lys409 by H-bonds; EV, with Arg71, Tyr74 and Lys409 by H-bonds; and VG, with Arg71, and Glu292 by H-bonds. Glutamic amino acid E (Ki = 694.05 uM) was revealed to stabilize bonds with _Rattus norvegicus_ mGluRuR1 key receptor residues from open-open conformation Tyr74, Arg78, Ser186, and Lys409. Tyr74, Arg78, Ser165, Ser186, Thr188, and Lys409 were calculated for the case of the dipeptide AH (Ki = 12.32 uM). The dipeptide DA (Ki = 322.75 uM) would interact with key residues Tyr74, Glu292, and Lys409; while DG (Ki = 424.75 uM), with Tyr74, Arg78, Ser186, Arg323, and Lys409.