Consolitate duplicate schlierf04 entries.

diff --git a/tex/src/root.bib b/tex/src/root.bib
index 57b3a6cdb2550aa9654305a85f09b7fcae5f6e53..6fadde99b12e0e518660955bc200456fb63c1585 100644 (file)
--- a/tex/src/root.bib
+++ b/tex/src/root.bib
@@ -632,44 +632,6 @@
   eprint =       "http://www.pnas.org/cgi/reprint/103/34/12724.pdf",
 }
 
-@Article{schlierf04,
-  author =       MSchlierf #" and "# HLi #" and "# JFernandez,
-  title =        "The unfolding kinetics of ubiquitin captured with
-                 single-molecule force-clamp techniques",
-  journal =      PNAS,
-  volume =       101,
-  number =       19,
-  pages =        "7299--7304",
-  year =         2004,
-  abstract =     "We use single-molecule force spectroscopy to study the
-                 kinetics of unfolding of the small protein ubiquitin.
-                 Upon a step increase in the stretching force, a
-                 ubiquitin polyprotein extends in discrete steps of 20.3
-                 {+/-} 0.9 nm marking each unfolding event. An average
-                 of the time course of these unfolding events was well
-                 described by a single exponential, which is a necessary
-                 condition for a memoryless Markovian process. Similar
-                 ensemble averages done at different forces showed that
-                 the unfolding rate was exponentially dependent on the
-                 stretching force. Stretching a ubiquitin polyprotein
-                 with a force that increased at a constant rate
-                 (force-ramp) directly measured the distribution of
-                 unfolding forces. This distribution was accurately
-                 reproduced by the simple kinetics of an all-or-none
-                 unfolding process. Our force-clamp experiments directly
-                 demonstrate that an ensemble average of ubiquitin
-                 unfolding events is well described by a two-state
-                 Markovian process that obeys the Arrhenius equation.
-                 However, at the single-molecule level, deviant behavior
-                 that is not well represented in the ensemble average is
-                 readily observed. Our experiments make an important
-                 addition to protein spectroscopy by demonstrating an
-                 unambiguous method of analysis of the kinetics of
-                 protein unfolding by a stretching force.",
-  doi =          "10.1073/pnas.0400033101",
-  URL =          "http://www.pnas.org/cgi/content/abstract/101/19/7299",
-  eprint =       "http://www.pnas.org/cgi/reprint/101/19/7299.pdf",
-}
 
 @Article{labeit03,
   author =       DLabeit #" and "# KWatanabe #" and "# CWitt #" and "#
@@ -5192,8 +5154,8 @@ doi = {10.1063/1.439715}
                  protein unfolding by a stretching force.",
   ISSN =         "0027-8424",
   doi =          "10.1073/pnas.0400033101",
-  url = "http://www.pnas.org/content/101/19/7299.abstract",
-  eprint = "http://www.pnas.org/content/101/19/7299.full.pdf",
+  URL =          "http://www.pnas.org/cgi/content/abstract/101/19/7299",
+  eprint =       "http://www.pnas.org/cgi/reprint/101/19/7299.pdf",
 }
 
 @Article{li03,