From: W. Trevor King <wking@tremily.us>
Date: Fri, 14 Jun 2013 04:05:14 +0000 (-0400)
Subject: root.bib: Add lee05 for EDC/linker background
X-Git-Tag: v1.0~77
X-Git-Url: http://git.tremily.us/?a=commitdiff_plain;h=7902725e21ae0499025ebb5d4c092a2bfb023b88;p=thesis.git

root.bib: Add lee05 for EDC/linker background
---

diff --git a/src/apparatus/sample-preparation.tex b/src/apparatus/sample-preparation.tex
index 56f8e06..06c9412 100644
--- a/src/apparatus/sample-preparation.tex
+++ b/src/apparatus/sample-preparation.tex
@@ -35,7 +35,7 @@ EGTA\citep{kellermayer03},
 Ni-NTA\citep{schmidt02,itoh04,sakaki05,berkemeier11}, or silanized
 glass\citep{sundberg03,ma10}.  Some groups have also functionalized
 the cantilever tips by coating them with molecules designed to bind to
-the protein.  Of these, a Ni-NTA coating is the most
+the protein\citep{lee05}.  Of these, a Ni-NTA coating is the most
 popular\citep{schmitt00}.
 %
 \nomenclature{EGTA}{Ethylene glycol tetraacetic acid}
diff --git a/src/cantilever/theory.tex b/src/cantilever/theory.tex
index 5bddcb1..09a38da 100644
--- a/src/cantilever/theory.tex
+++ b/src/cantilever/theory.tex
@@ -55,6 +55,7 @@ unfolding force, and for tensions $\sim 280\U{pN}$ is $\sim
 spring constants, so cantilever stiffness drives the effective spring
 constant for the first four domains, after which point I27 stiffness
 takes the lead.
+
 \begin{figure}
   \begin{tikzpicture}
     % Inspired by Florian Hollandt's RNA codons
@@ -73,6 +74,7 @@ takes the lead.
     \draw[doublebond] (Na) -- (Cc) -- (Nb);
     \draw (Nb) -- (Cd.center) -- (Ce.center) -- (Cf.center);
   \end{tikzpicture}%
-  \caption{EDC (TODO: full name)
-    \label{fig:EDC}}
+  \caption{1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC), a
+    short, stiff linker which has been used to bind proteins to gold
+    surfaces\cite{lee05}.\label{fig:EDC}}
 \end{figure}
diff --git a/src/root.bib b/src/root.bib
index 7a65ef1..725ad70 100644
--- a/src/root.bib
+++ b/src/root.bib
@@ -673,6 +673,7 @@
 @string{MMartin = "Martin, M. J."}
 @string{YMartin = "Martin, Y."}
 @string{HMassa = "Massa, H."}
+@string{MIT = "Massachusetts Institute of Technology"}
 @string{GAMatei = "Matei, G.~A."}
 @string{DMaterassi = "Materassi, Donatello"}
 @string{JMathe = "Math\'e, J\'er\^ome"}
@@ -7750,6 +7751,50 @@
         the different driving forces in protein folding."
 }
 
+@mastersthesis{ lee05,
+  author = SLee,
+  title = {Chemical Functionalization of AFM Cantilevers},
+  school = MIT,
+  year = 2005,
+  month = sep,
+  url = {http://dspace.mit.edu/handle/1721.1/34205},
+  abstract = {Atomic force microscopy (AFM) has been a powerful
+    instrument that provides nanoscale imaging of surface features,
+    mainly of rigid metal or ceramic surfaces that can be insulators
+    as well as conductors. Since it has been demonstrated that AFM
+    could be used in aqueous environment such as in water or various
+    buffers from which physiological condition can be maintained, the
+    scope of the application of this imaging technique has been
+    expanded to soft biological materials. In addition, the main usage
+    of AFM has been to image the material and provide the shape of
+    surface, which has also been diversified to molecular-recognition
+    imaging - functional force imaging through force spectroscopy and
+    modification of AFM cantilevers. By immobilizing of certain
+    molecules at the end of AFM cantilever, specific molecules or
+    functionalities can be detected by the combination of intrinsic
+    feature of AFM and chemical modification technique of AFM
+    cantilever. The surface molecule that is complementary to the
+    molecule at the end of AFM probe can be investigated via
+    specificity of molecule-molecule interaction.(cont.) Thus, this
+    AFM cantilever chemistry, or chemical functionalization of AFM
+    cantilever for the purpose of chemomechanical surface
+    characterization, can be considered as an infinite source of
+    applications important to understanding biological materials and
+    material interactions. This thesis is mainly focused on three
+    parts: (1) AFM cantilever chemistry that introduces specific
+    protocols in details such as adsorption method, gold chemistry,
+    and silicon nitride cantilever modification; (2) validation of
+    cantilever chemistry such as X-ray photoelectron spectroscopy
+    (XPS), AFM blocking experiment, and fluorescence microscopy,
+    through which various AFM cantilever chemistry is verified; and
+    (3) application of cantilever chemistry, especially toward the
+    potential of force spectroscopy and the imaging of biological
+    material surfaces.},
+  language = {eng},
+  note = {Binding proteins to gold-coated cantilevers via EDC (among
+    other things in this thesis.},
+}
+
 @article { walton08,
     author = EBWalton #" and "# SLee #" and "# KJVanVliet,
     title = "Extending {B}ell's model: How force transducer stiffness alters