Author: bugman
Date: Fri Mar 21 15:15:25 2008
New Revision: 5123
URL: http://svn.gna.org/viewcvs/relax?rev=5123&view=rev
Log:
Improved the reference page layout.
Modified:
website/refs.html
website/relax.css
Modified: website/refs.html
URL:
http://svn.gna.org/viewcvs/relax/website/refs.html?rev=5123&r1=5122&r2=5123&view=diff
==============================================================================
--- website/refs.html (original)
+++ website/refs.html Fri Mar 21 15:15:25 2008
@@ -63,25 +63,25 @@
<div class="main">
<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),
4989â4991.</li>
+ <ul class="ref_ul">
+ <li class="ref_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), 4989â4991.</li>
- <li id="dAuvergneGooley03">d'Auvergne, E. J. and Gooley, P. R. (2003).
The use of model selection in the
+ <li class="ref_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), 25â39. (<a
href="http://www.springerlink.com/content/g15p85235225v865/";>abstract</a>)</li>
- <li id="dAuvergneGooley06">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),
117â135. (<a
href="http://www.springerlink.com/content/lpr22t6704141464/";>abstract</a>)</li>
+ <li class="ref_li" id="dAuvergneGooley06">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), 117â135. (<a
href="http://www.springerlink.com/content/lpr22t6704141464/";>abstract</a>)</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 class="ref_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), 2674â2686.</li>
+ <li class="ref_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),
2674â2686.</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), 4546â4559.</li>
+ <li class="ref_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), 4546â4559.</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), 4559â4570.</li>
+ <li class="ref_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), 4559â4570.</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), 144â163.</li>
+ <li class="ref_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), 144â163.</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), 3055â3063.</li>
+ <li class="ref_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), 3055â3063.</li>
</ul>
</div>
Modified: website/relax.css
URL:
http://svn.gna.org/viewcvs/relax/website/relax.css?rev=5123&r1=5122&r2=5123&view=diff
==============================================================================
--- website/relax.css (original)
+++ website/relax.css Fri Mar 21 15:15:25 2008
@@ -153,6 +153,14 @@
font-style:italic;
}
+.ref_ul {
+ padding:0px;
+ list-style:none;
+}
+
+.ref_li {
+ margin-top:20px;
+}
a {
text-decoration:none;
r5123 - in /website: refs.html relax.css