Author: bugman
Date: Fri Mar 21 15:35:45 2008
New Revision: 5129
URL: http://svn.gna.org/viewcvs/relax?rev=5129&view=rev
Log:
Better spacing in the HTML.
Modified:
website/refs.html
Modified: website/refs.html
URL:
http://svn.gna.org/viewcvs/relax/website/refs.html?rev=5129&r1=5128&r2=5129&view=diff
==============================================================================
--- website/refs.html (original)
+++ website/refs.html Fri Mar 21 15:35:45 2008
@@ -64,14 +64,14 @@
<div class="main_box">
<h1>References</h1>
<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 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 class="ref_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://dx.doi.org/10.1023/A:1021902006114";>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://dx.doi.org/10.1007/s10858-006-9007-z";>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://dx.doi.org/10.1007/s10858-006-9007-z";>abstract</a>)</li>
- <li class="ref_li" id="dAuvergneGooley07">d'Auvergne E. J., Gooley P. R.
(2007). Set theory formulation of the model-free problem and the diffusion
seeded model-free paradigm. <em>Mol. Biosyst.</em>, <strong>3</strong>(7),
483-494. (<a href="dx.doi.org/10.1039/b702202f">abstract</a>)</li>
+ <li class="ref_li" id="dAuvergneGooley07">d'Auvergne E. J., Gooley P. R.
(2007). Set theory formulation of the model-free problem and the diffusion
seeded model-free paradigm. <em>Mol. Biosyst.</em>, <strong>3</strong>(7),
483-494. (<a href="dx.doi.org/10.1039/b702202f">abstract</a>)</li>
<li class="ref_li" id="dAuvergneGooley08a">d'Auvergne, E. J. and Gooley,
P. R. (2008). Optimisation of NMR dynamic models I. Minimisation algorithms
and their performance within the model-free and Brownian rotational diffusion
spaces. <em>J. Biomol. NMR</em>, <strong>40</strong>(2), 107-119. (<a
href="http://dx.doi.org/10.1007/s10858-007-9214-2";>abstract</a>)</li>
@@ -81,15 +81,15 @@
<li class="ref_li" id="Horne07">Horne J., d'Auvergne E. J., Coles M.,
Velkov T., Chin Y., Charman W. N., Prankerd R., Gooley P. R., Scanlon M. J.
(2007). Probing the flexibility of the DsbA oxidoreductase from <em>Vibrio
cholerae</em> - a <sup>15</sup>N-<sup>1</sup>H heteronuclear NMR relaxation
analysis of oxidized and reduced forms of DsbA. <em>J. Mol. Biol.</em>,
<strong>371</strong>(3), 703-716. (<a
href="http://dx.doi.org/10.1016/j.jmb.2007.05.067";>abstract</a>)</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 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 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 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 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 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 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 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 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>
+ <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>
r5129 - /website/refs.html