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<br>
<div align="center"><font size=5><b>Miercoles 5 de setiembre - 13
hs<br><br>
</b>Aula de Seminarios INQUIMAE-DQIAQF (3º piso Pab. II) <br><br>
<br>
</font><font size=6><b>Prof. Cecilia Clementi <br>
</font><font size=4><i>Department of Chemistry, Rice University, Houston,
USA</i></font><font size=6> <br><br>
<br>
</font><font size=5>"Multi-resolution protein modeling by combining
theory and experiment"<br><br>
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Abstract:<br>
The detailed characterization of the overall free energy landscape<br>
associated with the folding process of a protein is the ultimate goal
in<br>
protein folding studies. Modern experimental techniques provide<br>
accurate thermodynamic and kinetic measurements on restricted regions
of<br>
a protein landscape.<br>
Although simplified protein models can access larger regions of the<br>
landscape, they are oftentimes built on assumptions and
approximations<br>
that affect the accuracy of the results. We present new
methodologies<br>
that allows to combine the complementary strengths of theory and<br>
experiment for a more complete characterization of a protein folding<br>
landscape at multiple resolutions. Recent results and possible<br>
applications will be discussed.<br>
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