Author: bugman
Date: Tue Aug 28 19:32:54 2012
New Revision: 17366
URL: http://svn.gna.org/viewcvs/relax?rev=17366&view=rev
Log:
Added links for all abstracts via DOI numbers on
http://www.nmr-relax.com/refs.html.
Modified:
website/refs.html
Modified: website/refs.html
URL:
http://svn.gna.org/viewcvs/relax/website/refs.html?rev=17366&r1=17365&r2=17366&view=diff
==============================================================================
--- website/refs.html (original)
+++ website/refs.html Tue Aug 28 19:32:54 2012
@@ -49,24 +49,24 @@
<h3>Original Lipari-Szabo theory</h3>
<ul class="ref_ul">
- <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), 4546-4559.
(<a href="http://dx.doi.org/10.1021/ja00381a009";>abstract</a>)</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), 4559-4570.
(<a href="http://dx.doi.org/10.1021/ja00381a010";>abstract</a>)</li>
</ul>
<h3>Extended model-free theory</h3>
<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), 4989-4991. (<a
href="http://dx.doi.org/10.1021/ja00168a070";>abstract</a>)</li>
</ul>
<h3>Model-free model selection</h3>
<ul class="ref_ul">
- <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="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. (<a
href="http://dx.doi.org/10.1023/A:1021902006114";>abstract</a>)</li>
</ul>
<h3>Model-free model elimination</h3>
<ul class="ref_ul">
- <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), 117-135. (<a
href="http://dx.doi.org/10.1007/s10858-006-9007-z";>abstract</a>)</li>
</ul>
<h3>Model-free minimisation</h3>
@@ -98,23 +98,23 @@
<div class="main_h2" id="n_state">
<h2>The N-state model analyses</h2>
<ul class="ref_ul">
- <li class="ref_li" id="Sun11">Sun, H., d'Auvergne, E. J., Reinscheid,
U. M., Dias, L. C., Andrade, C. K. Z., Rocha, R. O., and Griesinger, C.
(2011). Bijvoet in solution reveals unexpected stereoselectivity in a michael
addition. <em>Chemistry-A European Journal</em>, <strong>17</strong>(6),
1811-1817.</li>
- <li class="ref_li" id="Erdelyi11">Erdelyi, M., d'Auvergne, E.,
Navarro-Vazquez, A., Leonov, A., and Griesinger, C. (2011). Dynamics of the
Glycosidic Bond: Conformational Space of Lactose. <em>Chemistry-A European
Journal</em>, <strong>17</strong>(34), 9368-9376.</li>
+ <li class="ref_li" id="Sun11">Sun, H., d'Auvergne, E. J., Reinscheid,
U. M., Dias, L. C., Andrade, C. K. Z., Rocha, R. O., and Griesinger, C.
(2011). Bijvoet in solution reveals unexpected stereoselectivity in a michael
addition. <em>Chemistry-A European Journal</em>, <strong>17</strong>(6),
1811-1817. (<a
href="http://dx.doi.org/10.1002/chem.201002520";>abstract</a>)</li>
+ <li class="ref_li" id="Erdelyi11">Erdelyi, M., d'Auvergne, E.,
Navarro-Vazquez, A., Leonov, A., and Griesinger, C. (2011). Dynamics of the
Glycosidic Bond: Conformational Space of Lactose. <em>Chemistry-A European
Journal</em>, <strong>17</strong>(34), 9368-9376. (<a
href="http://dx.doi.org/10.1002/chem.201100854";>abstract</a>)</li>
</ul>
</div>
<div class="main_h2" id="misc">
<h2>Misc.</h2>
<ul class="ref_ul">
- <li class="ref_li" id="Chen04"> Chen, J., Brooks, 3rd, C. L., and
Wright, P. E. (2004). Model-free analysis of protein dynamics: assessment of
accuracy and model selection protocols based on molecular dynamics
simulation. <em>J. Biomol. NMR</em>, <strong>29</strong>(3), 243-257.</li>
+ <li class="ref_li" id="Chen04"> Chen, J., Brooks, 3rd, C. L., and
Wright, P. E. (2004). Model-free analysis of protein dynamics: assessment of
accuracy and model selection protocols based on molecular dynamics
simulation. <em>J. Biomol. NMR</em>, <strong>29</strong>(3), 243-257. (<a
href="http://dx.doi.org/10.1023/b:jnmr.0000032504.70912.58";>abstract</a>)</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 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. (<a
href="http://dx.doi.org/10.1021/bi00003a021";>abstract</a>)</li>
<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), 2674-2686. (<a
href="http://dx.doi.org/10.1021/bi9526802";>abstract</a>)</li>
- <li class="ref_li" id="Mandel95">Mandel, A. M., Akke, M., and Palmer,
3rd, A. G. (1995). Backbone dynamics of <em>Escherichia coli</em>
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 <em>Escherichia coli</em>
ribonuclease HI: correlations with structure and function in an active
enzyme. <em>J. Mol. Biol.</em>, <strong>246</strong>(1), 144-163. (<a
href="http://dx.doi.org/10.1006/jmbi.1994.0073";>abstract</a>)</li>
</ul>
</div>
r17366 - /website/refs.html