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         <center><i>Figure 15. The structure of protein HpdR after molecular dynamics simulation bound to DNA PhpdH.</i></center>
         <p></p>
         <p>Later, we attempted to create PhpdH<span class="katex"><span class="katex-mathml"></span><span aria-hidden="true" class="katex-html"><span class="base"><span style="height:0.6833em;" class="strut"></span><span class="mord">Δ</span></span></span></span>SarJ, but due to equipment failure, we did not obtain the final experimental results. We re-analyzed using the same method and obtained the following results (Figure. 16).</p>
-        <p style="text-align: center;"><img src="https://static.igem.wiki/teams/5127/model/fig-model-hpdr-before-analysis.webp" style="width: 50%"><img src="https://static.igem.wiki/teams/5127/model/fig-model-hpdr-after-analysis.webp" style="width: 50%"></p>
+        <p style="text-align: center;"><img src="https://static.igem.wiki/teams/5127/model/before-analysis.webp" style="width: 50%"><img src="https://static.igem.wiki/teams/5127/model/fig-model-hpdr-after-analysis.webp" style="width: 50%"></p>
         <center><i>Figure 16. The structure of protein HpdR before/after MD bound to DNA PhpdHΔSarJ</i></center>
         <p></p>
         <p>We found that the protein docking score after 200ps of docking was somewhat lower compared to the protein-DNA docking score before the molecular dynamics simulation. Upon analyzing the active sites, we discovered that there was a noticeable release or a significant decrease in the bonding of nucleic acids in the RBS region. Therefore, we believe that SarJ is the cause of the experimental failure.</p>