Distinguish between glutamine and glutamic acid

This is important ;).  Thanks, Prof. Cruz.

diff --git a/src/apparatus/polymer-synthesis.tex b/src/apparatus/polymer-synthesis.tex
index a2795c0043e88d5e6d8e8b5b961248be10384965..31bbf3bd6b161a33996e93678d2c429f4b86174a 100644 (file)
--- a/src/apparatus/polymer-synthesis.tex
+++ b/src/apparatus/polymer-synthesis.tex
@@ -123,7 +123,8 @@ attracted to the metal ion.
 \nomenclature[text ]{Asn}{Asparagine, an amino acid.}
 \nomenclature[text ]{Asp}{Aspartic acid, an amino acid.}
 \nomenclature[text ]{Cys}{Cystine, an amino acid.}
-\nomenclature[text ]{Glu}{Glutamine, an amino acid.}
+\nomenclature[text ]{Glu}{Glutamic acid, an amino acid.}
+\nomenclature[text ]{Gln}{Glutamine, an amino acid.}
 \nomenclature[text ]{Gly}{Glycine, an amino acid.}
 \nomenclature[text ]{His}{Histidine, an amino acid.}
 \nomenclature[text ]{Ile}{Isoleucine, an amino acid.}

diff --git a/src/future/salt.tex b/src/future/salt.tex
index 8bbe12f052ee294ecf453d414d589b6f3ff98ee9..c7df0fb4d05262a92b2adc57295077f66f4974ab 100644 (file)
--- a/src/future/salt.tex
+++ b/src/future/salt.tex
@@ -6,7 +6,11 @@ strength of the buffer did significantly decrease the unfolding force
 (folding stability) of I27.  For labs with strong gene-splicing
 capability, it would be interesting to replace the glutamic acids
 involved in the major bonding (\cref{fig:I27:H-bonds}) with
-alternative groups to gauge the specificity of the effect.
+alternative groups to gauge the specificity of the effect.  For
+example, glutamine is identical to glutamic acid, except that it has a
+hydroxyl group (OH) in the side-chain where glutamic acid has an
+amine group (NH\textsubscript{2}).  This gives glutamine and glutamic
+acid similar steric properties, but very different chemistry.
 
 While the statistics are strong for the two concentrations we tested
 (standard PBS and PBS with an additional $0.5\U{M}$ \CaCl), it would