From: W. Trevor King <wking@tremily.us>
Date: Thu, 25 Apr 2013 17:10:31 +0000 (-0400)
Subject: introduction/main.tex: Expand on the landscape/pathway distinction
X-Git-Tag: v1.0~287
X-Git-Url: http://git.tremily.us/?a=commitdiff_plain;h=8140e0220cd9088087c7a49b8b093ed540f6cd0e;p=thesis.git

introduction/main.tex: Expand on the landscape/pathway distinction
---

diff --git a/src/introduction/main.tex b/src/introduction/main.tex
index f55709d..2fad3fd 100644
--- a/src/introduction/main.tex
+++ b/src/introduction/main.tex
@@ -52,15 +52,18 @@ remarkably difficult.
 \label{sec:energy-landscape}
 
 % the free energy landscape
-Folding a protein via a brute force sampling of all possible
-conformations is impossibly inefficient, due to the exponential
-scaling of possible conformations with protein length, as outlined by
-\citet{levinthal69}.  This has lead to a succession of models
-explaining the folding mechanism.  For a number of years, the
+Finding a protein's lowest energy state via a brute force sampling of
+all possible conformations is impossibly inefficient, due to the
+exponential scaling of possible conformations with protein length, as
+outlined by \citet{levinthal69}.  This has lead to a succession of
+models explaining the folding mechanism.  For a number of years, the
 ``pathway'' model of protein folding enjoyed popularity
 (\cref{fig:folding:pathway})\citep{levinthal69}.  More recently, the
 ``landscape'' or ``funnel'' model has come to the fore
-(\cref{fig:folding:landscape})\citep{dill97}.
+(\cref{fig:folding:landscape})\citep{dill97}.  Both of these models
+reduce the conformation space to a more approachable analog, and their
+success depends on striking a useful balance between simplicity and
+accuracy.
 
 \begin{figure}
   \begin{center}