Author: bugman Date: Fri Mar 21 15:06:25 2008 New Revision: 5122 URL: http://svn.gna.org/viewcvs/relax?rev=5122&view=rev Log: Added a link to the JBNMR abstract of the model elimination paper. Modified: website/refs.html Modified: website/refs.html URL: http://svn.gna.org/viewcvs/relax/website/refs.html?rev=5122&r1=5121&r2=5122&view=diff ============================================================================== --- website/refs.html (original) +++ website/refs.html Fri Mar 21 15:06:25 2008 @@ -65,14 +65,22 @@ <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> + <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.</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 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 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 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> </ul>