<h3>Title</h3>
<h3>Chaperonin nano-machines: allostery and function</h3>
<p><strong><span style="text-decoration: underline;">Abstract</span> :</strong></p>
<p style="text-align: justify;">Chaperonins are nano-machines that are built of two back-to-back stacked heptameric rings.  They assist protein folding by undergoing large conformational changes that are controlled by ATP binding and hydrolysis.  In the <em>E. coli</em> cell, only about 60 different proteins require GroEL for efficient folding.  In the first part of the talk, I will describe work that was aimed at determining the properties that distinguish GroEL clients from non-clients.  In the second part of the talk, I will describe new approaches for establishing allosteric mechanisms.  Using these approaches, it was possible to show that the chaperonin GroEL from <em>E. coli</em> undergoes concerted intra-ring conformational changes whereas its eukaryotic homologue CCT/TRiC undergoes sequential intra-ring conformational changes.  The impact of these different allosteric mechanisms on the folding functions of GroEL and CCT/TRiC will be discussed.</p>