Added dates to carrion-vazques99* which swapped a <-> b.

diff --git a/tex/src/cantilever/methods.tex b/tex/src/cantilever/methods.tex
index 373f0450691b200e996b378537685c8e0e214392..5ac0c5457e8b18d974489e7d51a42aa4d5f608d6 100644 (file)
--- a/tex/src/cantilever/methods.tex
+++ b/tex/src/cantilever/methods.tex
@@ -5,7 +5,7 @@ The experiments were carried out on octomers of I27 (\cref{fig:I27}).
 \nomenclature{I27}{Immunoglobulin-like domain 27 from human Titin}\index{I27}
 I27 is a model protein that has been used in mechanical unfolding
 experiments since the first use of synthetic
-chains\citep{carrion-vazquez99b,TODO}.  It was used here because it is
+chains\citep{carrion-vazquez99a,TODO}.  It was used here because it is
 both well characterized and readily available (%
 \href{http://www.athenaes.com/}{AthenaES}, Baltimore, MD,
 \href{http://www.athenaes.com/I27OAFMReferenceProtein.php}{0304}).

diff --git a/tex/src/cantilever/theory.tex b/tex/src/cantilever/theory.tex
index ae30cd91e5a84743d05dd7e93018d972fafa7ec0..7ab8b3160ffd77c75bd739cd3c2383efc6d2e1ce 100644 (file)
--- a/tex/src/cantilever/theory.tex
+++ b/tex/src/cantilever/theory.tex
@@ -26,7 +26,7 @@ tension.  The Bell-model unfolding rate is thus
 and stiffer linkers will increase the mean unfolding force.
 
 Unfolded I27 domains can be well-modeled as wormlike chains (WLCs,
-\cref{sec:tension:wlc})\citep{carrion-vazquez99b}, where $p \approx
+\cref{sec:tension:wlc})\citep{carrion-vazquez99a}, where $p \approx
 4\U{\AA}$ is the persistence length, and $L \approx 28\U{nm}$ is the
 contour length of the unfolded domain.  Obviously effective stiffness
 of an unfolded I27 domain is highly dependent on the unfolding force,

diff --git a/tex/src/introduction/main.tex b/tex/src/introduction/main.tex
index cd8e51057d4aed7abd1b287748d474c7e2f78194..1ba7befd6d0af28910ba79abc3e3cad4c8f5c676 100644 (file)
--- a/tex/src/introduction/main.tex
+++ b/tex/src/introduction/main.tex
@@ -116,7 +116,7 @@ microscopes\citep{halvorsen09}.  Of these mechanical manipulation
 methods, AFM is the most widely used due to the availability of
 user-friendly commercial instruments.  AFM has been employed on
 several types of biological macromolecules, mechanically unfolding
-proteins\citep{carrion-vazquez99b} and forcing structural transitions
+proteins\citep{carrion-vazquez99a} and forcing structural transitions
 in DNA\citep{rief99} and polysaccharides\citep{rief97b}.  An
 AFM\index{AFM} uses a sharp tip integrated at the end of a cantilever
 to interact with the sample.  Cantilever bending is measured by a
@@ -162,7 +162,7 @@ interactions between the AFM tip and the substrate may be stronger
 than the forces required to unfold the protein when the surfaces are a
 few nanometers apart.  To circumvent these difficulties, globular
 protein molecules are linked into polymers, which are then used in the
-AFM studies\citep{carrion-vazquez99b,chyan04,carrion-vazquez03}.  When
+AFM studies\citep{carrion-vazquez99a,chyan04,carrion-vazquez03}.  When
 such a polymer is pulled from its ends, each protein molecule feels
 the externally applied force, which increases the probability of
 unfolding by reducing the free energy barrier between the native and

diff --git a/tex/src/root.bib b/tex/src/root.bib
index 2203e0a40f711b064421bf11e8c73caca0dbc52b..f04841d72284be4aba66d70920933cb80453b18f 100644 (file)
--- a/tex/src/root.bib
+++ b/tex/src/root.bib
@@ -1838,11 +1838,30 @@
 }
 
 @article { carrion-vazquez99a,
+    author = MCarrionVazquez #" and "# AOberhauser #" and "# SFowler #" and "#
+        PMarszalek #" and "# SBroedel #" and "# JClarke #" and "# JFernandez,
+    title = "Mechanical and chemical unfolding of a single protein: A
+        comparison",
+    year = 1999,
+    month = mar,
+    day = 30,
+    journal = PNAS,
+    volume = 96,
+    number = 7,
+    pages = "3694--3699",
+    doi = "10.1073/pnas.96.7.3694",
+    eprint = "http://www.pnas.org/cgi/reprint/96/7/3694.pdf",
+    url = "http://www.pnas.org/cgi/content/abstract/96/7/3694"
+}
+
+@article { carrion-vazquez99b,
     author = MCarrionVazquez #" and "# PMarszalek #" and "# AOberhauser #" and
         "# JFernandez,
     title = "Atomic force microscopy captures length phenotypes in single
         proteins",
     year = 1999,
+    month = sep,
+    day = 28,
     journal = PNAS,
     volume = 96,
     number = 20,
@@ -1853,21 +1872,6 @@
     abstract = ""
 }
 
-@article { carrion-vazquez99b,
-    author = MCarrionVazquez #" and "# AOberhauser #" and "# SFowler #" and "#
-        PMarszalek #" and "# SBroedel #" and "# JClarke #" and "# JFernandez,
-    title = "Mechanical and chemical unfolding of a single protein: A
-        comparison",
-    year = 1999,
-    journal = PNAS,
-    volume = 96,
-    number = 7,
-    pages = "3694--3699",
-    doi = "10.1073/pnas.96.7.3694",
-    eprint = "http://www.pnas.org/cgi/reprint/96/7/3694.pdf",
-    url = "http://www.pnas.org/cgi/content/abstract/96/7/3694"
-}
-
 @article { chyan04,
     author = CLChyan #" and "# FCLin #" and "# HPeng #" and "# JMYuan #" and "#
         CHChang #" and "# SHLin #" and "# GYang,

diff --git a/tex/src/sawsim/introduction.tex b/tex/src/sawsim/introduction.tex
index a0522d95cc61ec7bbc6b00aa656c94b730ef9eef..aff4c4784452fa673489a35b13c6251be142d0d4 100644 (file)
--- a/tex/src/sawsim/introduction.tex
+++ b/tex/src/sawsim/introduction.tex
@@ -23,7 +23,7 @@ as the distance from the native state to the transition state along
 the pulling direction.  The Monte Carlo simulation method has been
 used since the first report of mechanical unfolding experiments using
 the AFM%
-\citep{rief97b,rief97a,rief98,carrion-vazquez99b,best02,zinober02,jollymore09},
+\citep{rief97b,rief97a,rief98,carrion-vazquez99a,best02,zinober02,jollymore09},
 but these previous implementations are neither fully described nor
 publicly available.
 

diff --git a/tex/src/unfolding-distributions/review.tex b/tex/src/unfolding-distributions/review.tex
index b561b058e8ca7a320a5c32611231ced013d8f6d6..5e45b1977d73c900da110ac2f779f0f66dc7ab57 100644 (file)
--- a/tex/src/unfolding-distributions/review.tex
+++ b/tex/src/unfolding-distributions/review.tex
@@ -5,7 +5,7 @@ There's not all that much information here, but it's a good place to go to get
 a big-picture overview before diving into the more technical papers.
 
 There are two main approaches to modeling protein domain unfolding under tension: Bell's and Kramers'\citep{schlierf06,dudko06,hummer03}.
-Bell introduced his model in the context of cell adhesion\citep{bell78}, but it has been widely used to model mechanical unfolding in proteins\citep{rief97a,carrion-vazquez99b,schlierf06} due to it's simplicity and ease of use\citep{hummer03}.
+Bell introduced his model in the context of cell adhesion\citep{bell78}, but it has been widely used to model mechanical unfolding in proteins\citep{rief97a,carrion-vazquez99a,schlierf06} due to it's simplicity and ease of use\citep{hummer03}.
 Kramers introduced his theory in the context of thermally activated barrier crossings, which is how we use it here.
 
 There is an excellent review of Kramers' theory in \citet{hanggi90}.