<p class="MsoNormal" align="center" style="margin-top:0in;margin-right:-26.0pt;
margin-bottom:0in;margin-left:-22.5pt;margin-bottom:.0001pt;text-align:center;
line-height:28.0pt;mso-pagination:none;mso-layout-grid-align:none;text-autospace:
none"><span style="font-size:20.0pt;font-family:ComicSansMS;color:#3B7C46"><b>Seminario
de Química Orgánica 2010</b></span><span style="font-size:20.0pt;font-family:
ArialMT"></span></p>
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line-height:14.0pt;mso-pagination:none;mso-layout-grid-align:none;text-autospace:
none"><span style="font-family:Garamond"><b> </b></span><span style="font-size:13.0pt;font-family:ArialMT"></span></p>
<p class="MsoNormal" align="center" style="margin-right:1.0pt;text-align:center;
line-height:20.0pt;mso-pagination:none;mso-layout-grid-align:none;text-autospace:
none"><span style="font-size:17.0pt;font-family:Garamond;color:#001078"><b>
Martes 6 de Abril de 2010 </b></span><span style="font-size:17.0pt;color:#001078"><b>―</b></span><span style="font-size:
17.0pt;font-family:Garamond;color:#001078"><b> 13:00 hora</b></span></p>
<p class="MsoNormal" align="center" style="margin-right:1.0pt;text-align:center;
line-height:20.0pt;mso-pagination:none;mso-layout-grid-align:none;text-autospace:
none"><span style="font-size:17.0pt;font-family:Garamond;color:#DA211F"><b>Aula
de Seminarios </b></span></p>
<p class="MsoNormal" align="center" style="margin-right:1.0pt;text-align:center;
line-height:20.0pt;mso-pagination:none;mso-layout-grid-align:none;text-autospace:
none"><span style="font-size:17.0pt;font-family:Garamond;color:#DA211F"><b>Departamento
de Química Orgánica</b></span><span style="font-size:13.0pt;font-family:ArialMT"></span></p>
<p class="MsoNormal" align="center" style="margin-right:1.0in;text-align:center;
line-height:14.0pt;mso-pagination:none;mso-layout-grid-align:none;text-autospace:
none"><span style="font-family:Garamond"><b> </b></span><span style="font-size:13.0pt;font-family:ArialMT"></span></p>
<p class="MsoNormal" align="center" style="margin-right:1.0in;text-align:center;
line-height:22.0pt;mso-pagination:none;mso-layout-grid-align:none;text-autospace:
none"><span style="font-size:19.0pt;font-family:Garamond"><b>
Expositora: Judith Frydman</b></span><span style="font-size:13.0pt;font-family:ArialMT"></span></p>
<p class="MsoNormal" align="center" style="text-align:center;mso-pagination:none;
mso-layout-grid-align:none;text-autospace:none"><span style="font-size:17.0pt;
font-family:Garamond"><b>Título:</b></span><span style="font-size:17.0pt;
font-family:ComicSansMS"><b> </b></span><span style="font-size:16.0pt;
font-family:Helvetica">Plegando y desplegando proteinas en condiciones normales
y patológicas</span></p>
<p class="MsoNormal" style="mso-pagination:none;mso-layout-grid-align:none;
text-autospace:none"><span style="font-family:Helvetica"> </span></p>
<p class="MsoNormal" style="text-align:justify;line-height:15.0pt;mso-line-height-rule:
exactly;mso-pagination:none;mso-layout-grid-align:none;text-autospace:none"><span style="font-family:Helvetica">Resumen: </span><span style="font-family:
Times-Roman"><b> </b></span><span style="font-family:Arial">Understanding
how proteins fold in the cell is a central problem in modern biology. The
transformation of the one-dimensional genetic information into
three-dimensional protein structures depends on the accuracy and efficiency of
the process of protein folding and the maintenance of this correct conformation
is essential for protein function and hence for the life of the cell.
While <i>in vitro</i></span><span style="font-family:Arial"> folding
experiments have shown that the process can occur spontaneously, it appears
that several protein families, generically termed molecular chaperones, are
required for the correct folding and assembly of proteins in the cell.
Despite considerable progress in the biochemical and biophysical analysis of
molecular chaperones, surprisingly little is known about how protein folding
occurs <i>in vivo,</i></span><span style="font-family:Arial"> following
translation by cytosolic ribosomes. Progress in this area has been hindered by
the lack of experimental approaches to study the folding intermediates of newly
translated proteins in the complex cellular environment found in both
translation lysates and intact cells. Our research aim is <u>to examine the
chaperone-interactions and folding intermediates of newly translated
polypeptides under physiological conditions.</u> By emphasizing folding
events as they occur at the ribosome during synthesis of a polypeptide we will
be able to understand the pathways of protein folding in eukaryotic cells and
how this folding is regulated. The research we carry out in the laboratory will
provide both conceptual and experimental tools to understand how proteins fold
in the cell. Considering that many folding-related diseases result from
very complex interactions between multiple cellular components, these tools
will prove essential to address mechanistic and cell biological questions.</span></p>
<p class="MsoNormal" style="text-align:justify;line-height:15.0pt;mso-line-height-rule:
exactly"><span style="font-family:Arial">Importantly, recent findings
indicating that the cellular accumulation of incorrectly folded proteins is the
molecular basis of many diseases, including Alzheimer's Disease, Prion Diseases
and Huntington Disease, underscore the importance of understanding the
mechanisms of folding <i>in vivo</i></span><span style="font-family:Arial">.
Alzheimer's and prion disease appear to be caused by the generation of a
"pathological" conformation in the newly translated protein that
would otherwise fold to a normal conformation that does not produce the
disease. In some model systems, molecular chaperones appear to play a
role in this conformational change. Thus, developing approaches to study
protein folding under physiological conditions is essential to understand how
folding defects can lead to disease.</span></p>
<p class="MsoNormal" style="text-align:justify;line-height:15.0pt;mso-line-height-rule:
exactly"><span style="font-family:Arial"> </span></p>