More key/name tuning in root.bib.

diff --git a/tex/src/root.bib b/tex/src/root.bib
index 7201015f6a64a6e3730e5607739f9c2c6cd56b03..7bdba8d60d9a2b19eabd95033907d6c95df1fd1f 100644 (file)
--- a/tex/src/root.bib
+++ b/tex/src/root.bib
@@ -2213,7 +2213,7 @@
 }
 
 @Article{makarov01,
-  author =       "Dmitrii E. Makarov and "# PHansma #" and Horia
+  author =       "Dmitrii E. Makarov"#" and "# PHansma #" and "#"Horia
                  Metiu",
   collaboration = "",
   title =        "Kinetic Monte Carlo simulation of titin unfolding",
@@ -3494,7 +3494,7 @@ doi = {10.1063/1.439715}
 
 @Book{vanKampen07,
   title = "Stochastic Processes in Physics and Chemistry",
-  author = "N.G. {van Kampen}",
+  author = "van Kampen, N.G.",
   edition = "3",
   publisher = "Elsevier, North-Holland Personal Library",
   address = "Amsterdam",
@@ -3932,8 +3932,8 @@ doi = {10.1063/1.439715}
 }
 
 @Article{kellermayer97,
-  author =       "M. S. Kellermayer and S. B. Smith and H. L. Granzier
-                 and "# CBustamante,
+  author =       "M. S. Kellermayer and S. B. Smith and H. L. Granzier"
+                 #" and "# CBustamante,
   title =        "Folding-unfolding transitions in single titin
                  molecules characterized with laser tweezers",
   journal =      SCI,
@@ -4625,7 +4625,8 @@ doi = {10.1063/1.439715}
 }
 
 @Article{dicola05,
-  author =       EDCola #" and Thomas A. Waigh and John Trinick
+  key = "diCola05",
+  author =       EDCola #" and "#"Thomas A. Waigh and John Trinick
                  and Larissa Tskhovrebova and Ahmed Houmeida and Wim
                  Pyckhout-Hintzen and Charles Dewhurst",
   title =        "Persistence length of titin from rabbit skeletal
@@ -5197,7 +5198,7 @@ doi = {10.1063/1.439715}
 }
 
 @Article{li05,
-  author =       "Lewyn Li and "# HHuang #" and "# CBadilla #"
+  author =       "Lewyn Li"#" and "# HHuang #" and "# CBadilla #"
                  and "# JFernandez,
   title =        "Mechanical unfolding intermediates observed by
                  single-molecule force spectroscopy in a fibronectin
@@ -5334,7 +5335,7 @@ note = "",
 issn = "0005-2728",
 doi = "10.1016/S0005-2728(03)00029-X",
 url = "http://dx.doi.org/10.1016/S0005-2728(03)00029-X",
-author = "Mikl\'os S. Z. Kellermayer and "# CBustamante #" and Henk L. Granzier",
+author = "Mikl\'os S. Z. Kellermayer"#" and "# CBustamante #" and "#"Henk L. Granzier",
   keywords = "Titin;Wormlike chain;Unfolding;Elasticity;AFM;Molecular force spectroscopy",
 abstract = "
 Titin is a giant polypeptide that spans half of the striated muscle sarcomere and generates passive force upon stretch. To explore the elastic response and structure of single molecules and oligomers of titin, we carried out molecular force spectroscopy and atomic force microscopy (AFM) on purified full-length skeletal-muscle titin. From the force data, apparent persistence lengths as long as ~1.5 nm were obtained for the single, unfolded titin molecule. Furthermore, data suggest that titin molecules may globally associate into oligomers which mechanically behave as independent wormlike chains (WLCs). Consistent with this, AFM of surface-adsorbed titin molecules revealed the presence of oligomers. Although oligomers may form globally via head-to-head association of titin, the constituent molecules otherwise appear independent from each other along their contour. Based on the global association but local independence of titin molecules, we discuss a mechanical model of the sarcomere in which titin molecules with different contour lengths, corresponding to different isoforms, are held in a lattice. The net force response of aligned titin molecules is determined by the persistence length of the tandemly arranged, different WLC components of the individual molecules, the ratio of their overall contour lengths, and by domain unfolding events. Biased domain unfolding in mechanically selected constituent molecules may serve as a compensatory mechanism for contour- and persistence-length differences. Variation in the ratio and contour length of the component chains may provide mechanisms for the fine-tuning of the sarcomeric passive force response."