From 6dfc17540386ae4e1b47b5049a96dc16112bdb80 Mon Sep 17 00:00:00 2001
From: Dreta <32196824+Dreta@users.noreply.github.com>
Date: Tue, 1 Oct 2024 15:28:27 +0900
Subject: [PATCH] fix capitalization of proper noun

---
 src/routes/description/+page.svelte | 20 +++++++++++++-------
 src/routes/engineering/+page.svelte | 10 +++++-----
 src/routes/results/+page.svelte     | 10 +++++-----
 3 files changed, 23 insertions(+), 17 deletions(-)

diff --git a/src/routes/description/+page.svelte b/src/routes/description/+page.svelte
index 49f3e3a..080a6ce 100644
--- a/src/routes/description/+page.svelte
+++ b/src/routes/description/+page.svelte
@@ -155,7 +155,7 @@
 <div class="flex justify-center">
     <img alt="Characteristics of mBaoJin" src={img7} />
 </div>
-<p class="slight">Figure 7. mBaojin has high pH stability: fluorescence pH stability was evaluated in the presence of
+<p class="slight">Figure 7. mBaoJin has high pH stability: fluorescence pH stability was evaluated in the presence of
     300 mM NaCl (n = 3 technical replicates each; squares, mean; error bars, s.d.; fluorescence was normalised to the
     maximum intensity value of the corresponding FP)</p>
 
@@ -197,10 +197,10 @@
         <p>In this study, we employed an innovative biosensing technology, the pCDH-AεB sensor. This sensor features
             a
             unique design that integrates the fluorescent protein Aquamarine with an optimized yellow fluorescent
-            protein (mBaojin), embedded within the epsilon domain of ATP synthase derived from Bacillus subtilis (ID
+            protein (mBaoJin), embedded within the epsilon domain of ATP synthase derived from Bacillus subtilis (ID
             AFQ603.1). Notably, the epsilon domain plays a crucial role in ATP binding; upon ATP interaction, it
             undergoes conformational changes that subsequently influence FRET efficiency. Under natural conditions,
-            without drug interference, the distance between Aquamarine and mBaojin remains relatively large,
+            without drug interference, the distance between Aquamarine and mBaoJin remains relatively large,
             resulting
             in a weak FRET effect. However, when cells are treated with anticancer drugs, fluctuations in
             intracellular
@@ -211,12 +211,18 @@
             a 96-well plate, simultaneously introducing various potential anticancer drugs into the co-culture
             system.
             Utilizing a high-content fluorescence detection system, we precisely measured the fluorescence emission
-            ratio between Aquamarine and mBaojin, enabling dynamic tracking of fluctuations in intracellular ATP
+            ratio between Aquamarine and mBaoJin, enabling dynamic tracking of fluctuations in intracellular ATP
             concentration following drug treatment. Specifically, the drug-induced changes in ATP levels triggered
             alterations in the spatial configuration of the epsilon domain, thereby modulating the FRET effect,
             which
-            can be visually reflected by subtle changes in mBaojin fluorescence intensity.</p>
-        <p>In the data analysis phase, we compared the differences in mBaojin fluorescence intensity between the
+            can be visually reflected by subtle changes in mBaoJin fluorescence intensity.</p>
+
+        <div class="flex justify-center lg:hidden">
+            <img alt="A flowchart of our processes" src={img9} />
+        </div>
+        <p class="slight lg:hidden">Figure 9. How mBaoJin takes effect</p>
+
+        <p>In the data analysis phase, we compared the differences in mBaoJin fluorescence intensity between the
             treatment group (with drug intervention) and the control group (without drug treatment) to evaluate the
             changes in intracellular ATP concentration induced by the drugs. This strategy effectively identifies
             potential anticancer compounds that can significantly regulate ATP levels.</p>
@@ -266,7 +272,7 @@
     <p>Lambert, T. (n.d.). Aquamarine at FPbase. <i>FPbase</i>. Retrieved from
         https://www.fpbase.org/protein/aquamarine/</p>
 
-    <p>Lambert, T. (n.d.). Mbaojin at FPbase. <i>FPbase</i>. Retrieved from https://www.fpbase.org/protein/mbaojin/</p>
+    <p>Lambert, T. (n.d.). Mbaojin at FPbase. <i>FPbase</i>. Retrieved from https://www.fpbase.org/protein/mBaoJin/</p>
 
     <p>Miyawaki, A. (2003). Visualization of the spatial and temporal dynamics of intracellular signaling. <i>Developmental
         Cell, 4</i>(3), 295–305. https://doi.org/10.1016/S1534-5807(03)00060-1</p>
diff --git a/src/routes/engineering/+page.svelte b/src/routes/engineering/+page.svelte
index 22cd3f5..b923b04 100644
--- a/src/routes/engineering/+page.svelte
+++ b/src/routes/engineering/+page.svelte
@@ -16,25 +16,25 @@
 </div>
 <p class="slight">Figure 1. FRET protein pairs were screened through FBbase FRET Calculator</p>
 
-<p>We selected two newly developed proteins: aquamarine as the donor and mBaojin as the acceptor. Aquamarine is a basic
+<p>We selected two newly developed proteins: aquamarine as the donor and mBaoJin as the acceptor. Aquamarine is a basic
     (constitutively fluorescent) cyan fluorescent protein published in 2013, derived from Aequorea
     Victoria. Its pKa is 3.3, indicating very low acid sensitivity and good stability in different pH environments.
     mBaoJin is a basic (constitutively fluorescent) green fluorescent protein published in 2024, derived from Cytaeis
     uchidae. It is reported to be a very rapidly maturing monomer with low acid sensitivity.</p>
 
 <p>We made this choice because the emission spectrum of aquamarine significantly overlaps with the excitation spectrum
-    of mbaojin, as shown in the graph, the spectral overlap integral value is 2.85 × 10⁻¹⁵ cm⁶ nm⁴, which is high,
+    of mBaoJin, as shown in the graph, the spectral overlap integral value is 2.85 × 10⁻¹⁵ cm⁶ nm⁴, which is high,
     indicating that a substantial portion of the donor’s emission falls within the acceptor’s range. This number is a
     key determinant of FRET efficiency. Moreover, the Förster distance is 60.21Å, which represents the distance at FRET
-    efficiency is 50%. Additionally, compared to the traditional FRET pairs, such as CFP-YFP, the overlap for mBaojin
+    efficiency is 50%. Additionally, compared to the traditional FRET pairs, such as CFP-YFP, the overlap for mBaoJin
     and T Aquamarine is more extensive, suggesting that this pair may produce stronger FRET signals. At the same time,
     the emission spectra of the donor and acceptor remain distinct, minimizing spectral interference and making it easy
     to distinguish the FRET signal from the donor and acceptor fluorescence. </p>
 
 <div class="flex justify-center">
-    <img alt="Visualization of the protein structures of mBaojin (left) and aquamarine (right)" src={img2} />
+    <img alt="Visualization of the protein structures of mBaoJin (left) and aquamarine (right)" src={img2} />
 </div>
-<p class="slight">Figure 2. Visualization of the protein structures of mBaojin (left) and aquamarine (right)</p>
+<p class="slight">Figure 2. Visualization of the protein structures of mBaoJin (left) and aquamarine (right)</p>
 
 <div class="flex justify-center">
     <img alt="Simulating FRET protein pairs" src={img3} />
diff --git a/src/routes/results/+page.svelte b/src/routes/results/+page.svelte
index 67c8e5c..3ff7d6a 100644
--- a/src/routes/results/+page.svelte
+++ b/src/routes/results/+page.svelte
@@ -13,17 +13,17 @@
 </script>
 
 <h2 class="heading-2" id="atp">Construction of ATP Biosensor</h2>
-<p>We selected two newly developed proteins: aquamarine as the donor and mBaojin as the acceptor. Aquamarine is a basic
+<p>We selected two newly developed proteins: aquamarine as the donor and mBaoJin as the acceptor. Aquamarine is a basic
     (constitutively fluorescent) cyan fluorescent protein published in 2013, derived from Aequorea
     Victoria. Its pKa is 3.3, indicating very low acid sensitivity and good stability in different pH environments.
     mBaoJin is a basic (constitutively fluorescent) green fluorescent protein published in 2024, derived from Cytaeis
     uchidae. It is reported to be a very rapidly maturing monomer with low acid sensitivity.</p>
 
 <p>We made this choice because the emission spectrum of aquamarine significantly overlaps with the excitation spectrum
-    of mbaojin, as shown in the graph, the spectral overlap integral value is 2.85 × 10⁻¹⁵ cm⁶ nm⁴, which is high,
+    of mBaoJin, as shown in the graph, the spectral overlap integral value is 2.85 × 10⁻¹⁵ cm⁶ nm⁴, which is high,
     indicating that a substantial portion of the donor’s emission falls within the acceptor’s range. This number is a
     key determinant of FRET efficiency. Moreover, the Förster distance is 60.21Å, which represents the distance at FRET
-    efficiency is 50%. Additionally, compared to the traditional FRET pairs, such as CFP-YFP, the overlap for mBaojin
+    efficiency is 50%. Additionally, compared to the traditional FRET pairs, such as CFP-YFP, the overlap for mBaoJin
     and T Aquamarine is more extensive, suggesting that this pair may produce stronger FRET signals. At the same time,
     the emission spectra of the donor and acceptor remain distinct, minimizing spectral interference and making it easy
     to distinguish the FRET signal from the donor and acceptor fluorescence. </p>
@@ -34,9 +34,9 @@
 <p class="slight">Figure 1. FRET protein pairs were screened through FBbase FRET Calculator</p>
 
 <div class="flex justify-center">
-    <img alt="Visualization of the protein structures of mBaojin (left) and aquamarine (right)" src={img2} />
+    <img alt="Visualization of the protein structures of mBaoJin (left) and aquamarine (right)" src={img2} />
 </div>
-<p class="slight">Figure 2. Visualization of the protein structures of mBaojin (left) and aquamarine (right)</p>
+<p class="slight">Figure 2. Visualization of the protein structures of mBaoJin (left) and aquamarine (right)</p>
 
 <div class="flex justify-center">
     <img alt="Simulating FRET protein pairs" src={img3} />
-- 
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