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Posted by edward on January 08, 2007 - 12:26:
Author: bugman
Date: Mon Jan  8 12:26:13 2007
New Revision: 2971

URL: http://svn.gna.org/viewcvs/relax?rev=2971&view=rev
Log:
Changed the "id" attribute values to be enclosed in quotes.

This problem was found using http://validator.w3.org.


Modified:
    website/refs.html

Modified: website/refs.html
URL: 
http://svn.gna.org/viewcvs/relax/website/refs.html?rev=2971&r1=2970&r2=2971&view=diff
==============================================================================
--- website/refs.html (original)
+++ website/refs.html Mon Jan  8 12:26:13 2007
@@ -63,16 +63,16 @@
  <div class="main_box">
   <h1>References</h1>
    <ul>
-    <li id=Clore90>Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, 
P. C., and Gronenborn, A. M. (1990b). Deviations from the simple 2-parameter 
model-free approach to the interpretation of N-15 nuclear magnetic-relaxation 
of proteins. <em>J. Am. Chem. Soc.</em>, <strong>112</strong>(12), 
4989–4991.</li>
-    <li id=dAuvergneGooley03>d'Auvergne, E. J. and Gooley, P. R. (2003). The 
use of model selection in the
+    <li id="Clore90">Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, 
P. C., and Gronenborn, A. M. (1990b). Deviations from the simple 2-parameter 
model-free approach to the interpretation of N-15 nuclear magnetic-relaxation 
of proteins. <em>J. Am. Chem. Soc.</em>, <strong>112</strong>(12), 
4989–4991.</li>
+    <li id="dAuvergneGooley03">d'Auvergne, E. J. and Gooley, P. R. (2003). 
The use of model selection in the
 model-free analysis of protein dynamics. <em>J. Biomol. NMR</em>, 
<strong>25</strong>(1), 25–39.</li>
-    <li id=dAuvergneGooley03>d'Auvergne, E. J. and Gooley, P. R. (2006). 
Model-free model elimination: A new step in the model-free dynamic analysis 
of NMR relaxation data. <em>J. Biomol. NMR</em>, <strong>35</strong>(2), 
117–135.</li>
-    <li id=Farrow95>Farrow, N. A., Zhang, O., Forman-Kay, J. D., Kay, L. E. 
(1995).  Comparison of the backbone dynamics of a folded and an unfolded SH3 
domain existing in equilibrium in aqueous buffer. <em>Biochem.</em>, 
<strong>34</strong>(3), 868-878.</li>
-    <li id=Lefevre96>Lefevre, J. F., Dayie, K. T., Peng, J. W., and Wagner, 
G. (1996). Internal mobility in the partially folded DNA binding and 
dimerization domains of GAL4: NMR analysis of the N-H spectral density 
functions. <em>Biochem.</em>, <strong>35</strong>(8), 2674–2686.</li>
-    <li id=LipariSzabo82a>Lipari, G. and Szabo, A. (1982a). Model-free 
approach to the interpretation of nuclear magnetic-resonance relaxation in 
macromolecules I. Theory and range of validity. <em>J. Am. Chem. Soc.</em>, 
<strong>104</strong>(17), 4546–4559.</li>
-    <li id=LipariSzabo82b>Lipari, G. and Szabo, A. (1982b). Model-free 
approach to the interpretation of nuclear magnetic-resonance relaxation in 
macromolecules II. Analysis of experimental results. <em>J. Am. Chem. 
Soc.</em>, <strong>104</strong>(17), 4559–4570.</li>
-    <li id=Mandel95>Mandel, A. M., Akke, M., and Palmer, 3rd, A. G. (1995). 
Backbone dynamics of Escherichia coli ribonuclease HI: correlations with 
structure and function in an active enzyme. <em>J. Mol. Biol.</em>, 
<strong>246</strong>(1), 144–163.</li>
-    <li id=Tugarinov01>Tugarinov, V., Liang, Z., Shapiro, Y. E., Freed, J. 
H., and Meirovitch, E. (2001). A structural mode-coupling approach to 
<sup>15</sup>N NMR relaxation in proteins. <em>J. Am. Chem. Soc.</em>, 
<strong>123</strong>(13), 3055–3063.</li>
+    <li id="dAuvergneGooley03">d'Auvergne, E. J. and Gooley, P. R. (2006). 
Model-free model elimination: A new step in the model-free dynamic analysis 
of NMR relaxation data. <em>J. Biomol. NMR</em>, <strong>35</strong>(2), 
117–135.</li>
+    <li id="Farrow95">Farrow, N. A., Zhang, O., Forman-Kay, J. D., Kay, L. 
E. (1995).  Comparison of the backbone dynamics of a folded and an unfolded 
SH3 domain existing in equilibrium in aqueous buffer. <em>Biochem.</em>, 
<strong>34</strong>(3), 868-878.</li>
+    <li id="Lefevre96">Lefevre, J. F., Dayie, K. T., Peng, J. W., and 
Wagner, G. (1996). Internal mobility in the partially folded DNA binding and 
dimerization domains of GAL4: NMR analysis of the N-H spectral density 
functions. <em>Biochem.</em>, <strong>35</strong>(8), 2674–2686.</li>
+    <li id="LipariSzabo82a">Lipari, G. and Szabo, A. (1982a). Model-free 
approach to the interpretation of nuclear magnetic-resonance relaxation in 
macromolecules I. Theory and range of validity. <em>J. Am. Chem. Soc.</em>, 
<strong>104</strong>(17), 4546–4559.</li>
+    <li id="LipariSzabo82b">Lipari, G. and Szabo, A. (1982b). Model-free 
approach to the interpretation of nuclear magnetic-resonance relaxation in 
macromolecules II. Analysis of experimental results. <em>J. Am. Chem. 
Soc.</em>, <strong>104</strong>(17), 4559–4570.</li>
+    <li id="Mandel95">Mandel, A. M., Akke, M., and Palmer, 3rd, A. G. 
(1995). Backbone dynamics of Escherichia coli ribonuclease HI: correlations 
with structure and function in an active enzyme. <em>J. Mol. Biol.</em>, 
<strong>246</strong>(1), 144–163.</li>
+    <li id="Tugarinov01">Tugarinov, V., Liang, Z., Shapiro, Y. E., Freed, J. 
H., and Meirovitch, E. (2001). A structural mode-coupling approach to 
<sup>15</sup>N NMR relaxation in proteins. <em>J. Am. Chem. Soc.</em>, 
<strong>123</strong>(13), 3055–3063.</li>
    </ul>
 
  </div>




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