Add new citation ng07b and change ng07 to ng07a.

diff --git a/src/root.bib b/src/root.bib
index f7bac1c7fa4b7e9a404aef6d43d2da9c3b2f5f02..c731c12bad82873ff2f9ccb63e9924571fd9cfeb 100644 (file)
--- a/src/root.bib
+++ b/src/root.bib
@@ -4993,12 +4993,14 @@
     project = "Energy Landscape Roughness"
 }
 
-@article { ng07,
+@article { ng07a,
     author = SNg #" and "# KBillings #" and "# TOhashi #" and "# MAllen #" and
         "# RBest #" and "# LRandles #" and "# HErickson #" and "# JClarke,
     title = "Designing an extracellular matrix protein with enhanced mechanical
         stability",
     year = 2007,
+               month = jun,
+               day = 5,
     journal = PNAS,
     volume = 104,
     number = 23,
@@ -5029,6 +5031,47 @@
         functional surface interactions."
 }
 
+@article { ng07b,
+    author = SNg #" and "# JClarke,
+    title = "Experiments Suggest that Simulations May Overestimate
+        Electrostatic Contributions to the Mechanical Stability of a
+        Fibronectin Type {III} Domain",
+    journal = JMB,
+    volume = 371,
+    number = 4,
+    pages = "851–854",
+    year = 2007,
+               month = aug,
+               day = 24,
+    issn = "0022-2836",
+    doi = "10.1016/j.jmb.2007.06.015",
+    url = "http://www.sciencedirect.com/science/article/pii/S0022283607007966",
+    keywords = "AFM",
+    keywords = "MD simulations",
+    keywords = "titin",
+    keywords = "forced unfolding",
+    keywords = "extracellular matrix",
+    abstract = "Steered molecular dynamics simulations have previously
+        been used to investigate the mechanical properties of the
+        extracellular matrix protein fibronectin. The simulations
+        suggest that the mechanical stability of the tenth type III
+        domain from fibronectin (FNfn10) is largely determined by a
+        number of critical hydrogen bonds in the peripheral
+        strands. Interestingly, the simulations predict that lowering
+        the pH from 7 to ∼4.7 will increase the mechanical stability
+        of FNfn10 significantly (by ∼33 %) due to the protonation of a
+        few key acidic residues in the A and B strands. To test this
+        simulation prediction, we used single-molecule atomic force
+        microscopy (AFM) to investigate the mechanical stability of
+        FNfn10 at neutral pH and at lower pH where these key residues
+        have been shown to be protonated. Our AFM experimental results
+        show no difference in the mechanical stability of FNfn10 at
+        these different pH values. These results suggest that some
+        simulations may overestimate the role played by electrostatic
+        interactions in determining the mechanical stability of
+        proteins."
+}
+
 @article { nome07,
     author = RNome #" and "# JZhao #" and "# WHoff #" and "# NScherer,
     title = "Axis-dependent anisotropy in protein unfolding from integrated
@@ -7054,4 +7097,3 @@
         configurations, of the order of a few kT, can reduce Levinthal's time
         to a biologically significant size."
 }
-