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<div>Dear All:</div>
<div>I am hosting a special biophysics/biochemistry talk in <b>1080 (Robert Smith seminar room) Physica Research Building (PRB) at 4pm today (March 29)</b>. The speaker is Prof. Amnon Horovitz from Dept. of Structural Biology, Weizmann Institute of Science
(<a href="https://www.weizmann.ac.il/Structural_Biology/Horovitz">https://www.weizmann.ac.il/Structural_Biology/Horovitz</a>/). Prof. Horovitz is well known on studies of protein allostery in complex systems. He used a variety of biophysical tools: mass spectrometry,
single-molecue, structural tools, etc… Please join us for this exciting seminar. </div>
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<div>The talk title and abstract is s follows:</div>
<div><b class="" style="font-family: Calibri; line-height: 21px; text-align: justify;"><br>
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<div><b class="" style="font-family: Calibri; line-height: 21px; text-align: justify;">Allostery in chaperonins: how and why</b></div>
<div><span class="" style="font-family: Calibri; line-height: 21px; text-align: justify;">Chaperonins </span><span class="" style="font-family: Calibri; line-height: 21px; text-align: justify;">consist of two back-to-back stacked heptameric rings with a cavity
at each end</span><span style="font-family: Calibri; line-height: 21px; text-align: justify;"> where protein folding can take place. They</span><span class="" style="font-family: Calibri; line-height: 21px; text-align: justify;"> assist protein folding by
undergoing large conformational changes that are controlled by ATP binding and hydrolysis. The concerted Monod–Wyman–Changeux and sequential Koshland–Némethy–Filmer models of cooperativity are often used to describe such allosteric switching. In general,
however, it has been impossible to distinguish between these different allosteric models using ensemble measurements of ligand binding in bulk protein solutions. In this talk, </span><span class="" style="font-family: Calibri; line-height: 21px; text-align: justify;">two
approaches </span><span class="" style="font-family: Calibri; line-height: 21px; text-align: justify;">that break this impasse will be described: one that is kinetic and a second that is based on native mass spectrometry. Using these approaches, it was possible
to show that the chaperonin GroEL from <i class="">E. coli</i> undergoes concerted intra-ring conformational changes whereas its eukaryotic homologue CCT/TRiC undergoes sequential intra-ring conformational changes.</span><span style="font-family: Calibri; line-height: 21px; text-align: justify;">
The impact of these different allosteric mechanisms on the folding functions of GroEL and CCT/TRiC will be discussed.</span></div>
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<div>Best regards,</div>
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<div><br>
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<div>Dongping Zhong</div>
<div>Robert Smith Professor of Physics</div>
<div>Professor of Chemistry and Biochemistry</div>
<div>The Ohio State University</div>
<div>Tel: 614-292-3044</div>
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