diff --git a/tex/discussion.tex b/tex/discussion.tex
index 9fe5f5b..3ea795c 100644
--- a/tex/discussion.tex
+++ b/tex/discussion.tex
@@ -17,13 +17,13 @@
 %\subsection{LSPR response to BSA}
 
 Figure \ref{fig:2pz_response} shows a red shift of the plasmon resonance frequency peak in presence of the BSA proteins.
-This result agrees with experimental observations
-\cite{TangETal2010, RaphaelETal2013}. Moreover, we observe a decrement of 
-the peak, which is also present in the results of Tang, et al.~\cite{TangETal2010}.
-Both results, the red-shift and the decrement of the peak in the presence of 
-the proteins, indicate that our boundary element method approach using electrostatic
-approximation is capable of capturing the characteristic resonance-frequency 
-shift in LSPR biosensors.
+Experimental observations of Tang, et al.~\cite{TangETal2010} with silver nanoparticles of approximately 17 nm in diameter and BSA proteins in solution revealed a red shift upon adding the proteins. 
+Similar to the effect we see with our model, they observed as well a decrement of 
+the peak amplitude.
+Other experimental results are consistent \cite{RaphaelETal2013}, with a red shift and decrease of the peak amplitude in the presence of the proteins.
+Our boundary element method approach using electrostatic
+approximation is thus able to capture the characteristic resonance-frequency 
+shift of LSPR biosensors.
 
 With the electric field aligned in the $z$-direction, placing the proteins at a distance
 in the $x$ or $y$ directions from the nanoparticle shows a negligible shift in the