[Todos] Seminario especial: Judith Frydman - Martes 6 de Abril 13 hs - Departamento de Química Orgánica

[Elizabeth Jares-Erijman]

*Seminario de Química Orgánica 2010*

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*        Martes 6 de Abril de 2010 **--** 13:00 hora*

*Aula de Seminarios *

*Departamento de Química Orgánica*

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*              Expositora: Judith Frydman*

*Título:** *Plegando y desplegando proteinas en condiciones normales y
patológicas



Resumen:  * *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 *in vitro* 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 *in vivo,* 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 *to examine the chaperone-interactions and folding
intermediates of newly translated polypeptides under physiological
conditions.*  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.

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 *in
vivo*.  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.
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