Use \subref in unfolding pathway vs. landscape image.

This is better than hardcoding subfigure references in the caption.

Also reference kellermayer97 as an early example of force spectroscopy
on proteins with laser tweezers (they're right after rief97a in the
journal).

diff --git a/src/introduction/main.tex b/src/introduction/main.tex
index 0323e4fef09efb242912d480d31e85bc70100f3c..e9ee8c589e030191ca68956d49b07a2bfaaaecca 100644 (file)
--- a/src/introduction/main.tex
+++ b/src/introduction/main.tex
@@ -83,15 +83,16 @@ explaining the folding mechanism.  For a number of years, the
   % \hspace{.25in}%
   \subfloat[][]{\includegraphics[width=2in]{figures/schematic/dill97-fig4}%
     \label{fig:folding:landscape}}
-  \caption{(a) A ``double T'' example of the pathway model of protein
-    folding, in which the protein proceeds from the native state $N$
-    to the unfolded state $U$ via a series of metastable transition
-    states $I_1$ and $I_2$ with two ``dead end'' states $I_1^X$ and
-    $I_2^X$.  Adapted from \citet{bedard08}.  (b) The landscape model
-    of protein folding, in which the protein diffuses through a
-    multi-dimensional free energy landscape.  Separate folding
-    attempts may take many distinct routes through this landscape on
-    the way to the folded state.  Reproduced from \citet{dill97}.
+  \caption{\subref{fig:folding:pathway} A ``double T'' example of the
+    pathway model of protein folding, in which the protein proceeds
+    from the native state $N$ to the unfolded state $U$ via a series
+    of metastable transition states $I_1$ and $I_2$ with two ``dead
+    end'' states $I_1^X$ and $I_2^X$.  Adapted from \citet{bedard08}.
+    \subref{fig:folding:landscape} The landscape model of protein
+    folding, in which the protein diffuses through a multi-dimensional
+    free energy landscape.  Separate folding attempts may take many
+    distinct routes through this landscape on the way to the folded
+    state.  Reproduced from \citet{dill97}.
     \label{fig:folding}}
   \end{center}
 \end{figure}
@@ -139,10 +140,11 @@ Single molecule techniques for manipulating biopolymers include
 optical measurements, \ie, single molecule fluorescence microscopy and
 spectroscopy, and mechanical manipulations of individual
 macromolecules, \ie, force microscopy and spectroscopy using atomic
-force microscopes (AFMs), laser tweezers\citep{forde02}, magnetic
-tweezers\citep{smith92}, biomembrane force probes\citep{merkel99}, and
-centrifugal microscopes\citep{halvorsen09}.  These techniques cover a
-wide range of approaches, and even when the basic approach is the same
+force microscopes (AFMs), laser tweezers\citep{kellermayer97,forde02},
+magnetic tweezers\citep{smith92}, biomembrane force
+probes\citep{merkel99}, and centrifugal
+microscopes\citep{halvorsen09}.  These techniques cover a wide range
+of approaches, and even when the basic approach is the same
 (e.g.\ force microscopy), the different techniques span orders of
 magnitude in the range of their controllable parameters.
 \nomenclature{AFM}{Atomic Force Microscope (or Microscopy)}