<html>
<head>
<meta http-equiv="Content-Type" content="text/html; charset=Windows-1252">
</head>
<body style="word-wrap: break-word; -webkit-nbsp-mode: space; -webkit-line-break: after-white-space; color: rgb(0, 0, 0); font-size: 14px; font-family: Calibri, sans-serif;">
<div>
<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 tomorrow (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>
<div><br>
</div>
<div>The talk title and abstract is s follows:</div>
<div><b class="" style="font-family: Calibri; line-height: 21px; text-align: justify;"><br>
</b></div>
<div><b class="" style="font-family: Calibri; line-height: 21px; text-align: justify;">Allostery in chaperonins: how and why</b></div>
<div>
<p class="MsoNormal" style="font-family: Calibri; text-align: justify; line-height: 21px;">
<span class="">Chaperonins </span><span class="">consist of two back-to-back stacked heptameric rings with a cavity at each end</span> where protein folding can take place. They<span class=""> 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="">two approaches </span><span class="">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> The impact of these different allosteric mechanisms on the folding functions of GroEL and CCT/TRiC will be discussed.</p>
</div>
<div><br>
</div>
<div>Best regards,</div>
<div></div>
<div>Best regards,</div>
<div>
<div><br>
</div>
<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>
<div>-------------------------------------------------------------------</div>
<div><br>
</div>
</div>
</div>
<div><br>
</div>
<span id="OLK_SRC_BODY_SECTION">
<div style="font-family:Calibri; font-size:11pt; text-align:left; color:black; BORDER-BOTTOM: medium none; BORDER-LEFT: medium none; PADDING-BOTTOM: 0in; PADDING-LEFT: 0in; PADDING-RIGHT: 0in; BORDER-TOP: #b5c4df 1pt solid; BORDER-RIGHT: medium none; PADDING-TOP: 3pt">
<span style="font-weight:bold">From: </span>Cmbp-trainers <<a href="mailto:cmbp-trainers-bounces+dongping=physics.osu.edu@lists.osu.edu">cmbp-trainers-bounces+dongping=physics.osu.edu@lists.osu.edu</a>> on behalf of "<a href="mailto:dongping@physics.osu.edu">dongping@physics.osu.edu</a>"
<<a href="mailto:dongping@physics.osu.edu">dongping@physics.osu.edu</a>><br>
<span style="font-weight:bold">Date: </span>Monday, March 27, 2017 at 11:19 PM<br>
<span style="font-weight:bold">To: </span>cbc-local-faculty <<a href="mailto:cbc-local-faculty-bounces@lists.osu.edu">cbc-local-faculty-bounces@lists.osu.edu</a>>, physics-faculty-full <<a href="mailto:physics-faculty-full-bounces@lists.osu.edu">physics-faculty-full-bounces@lists.osu.edu</a>>,
"<a href="mailto:physics-faculty-associate@lists.osu.edu">physics-faculty-associate@lists.osu.edu</a>" <<a href="mailto:physics-faculty-associate@lists.osu.edu">physics-faculty-associate@lists.osu.edu</a>>, "<a href="mailto:cbc-everyone@groups.asc.ohio-state.edu">cbc-everyone@groups.asc.ohio-state.edu</a>"
<<a href="mailto:cbc-everyone@groups.asc.ohio-state.edu">cbc-everyone@groups.asc.ohio-state.edu</a>>, "<a href="mailto:physics-all@lists.osu.edu">physics-all@lists.osu.edu</a>" <<a href="mailto:physics-all@lists.osu.edu">physics-all@lists.osu.edu</a>>, Biophysics
Faculty <<a href="mailto:biophys-fac@cannoli.mps.ohio-state.edu">biophys-fac@cannoli.mps.ohio-state.edu</a>><br>
<span style="font-weight:bold">Cc: </span>"<a href="mailto:biophys-grad@cannoli.mps.ohio-state.edu">biophys-grad@cannoli.mps.ohio-state.edu</a>" <<a href="mailto:biophys-grad@cannoli.mps.ohio-state.edu">biophys-grad@cannoli.mps.ohio-state.edu</a>>, "<a href="mailto:'cmbp-trainees@lists.osu.edu">'cmbp-trainees@lists.osu.edu</a>'"
<<a href="mailto:cmbp-trainees@lists.osu.edu">cmbp-trainees@lists.osu.edu</a>>, "<a href="mailto:'osbp_student@lists.osu.edu">'osbp_student@lists.osu.edu</a>'" <<a href="mailto:osbp_student@lists.osu.edu">osbp_student@lists.osu.edu</a>>, "<a href="mailto:'cmbp-trainers@lists.osu.edu">'cmbp-trainers@lists.osu.edu</a>'"
<<a href="mailto:cmbp-trainers@lists.osu.edu">cmbp-trainers@lists.osu.edu</a>>, "<a href="mailto:'osbp_faculty@lists.osu.edu">'osbp_faculty@lists.osu.edu</a>'" <<a href="mailto:osbp_faculty@lists.osu.edu">osbp_faculty@lists.osu.edu</a>><br>
<span style="font-weight:bold">Subject: </span>[Cmbp-trainers] special biophysics/biochemistry seminar from Dongping<br>
</div>
<div><br>
</div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
Dear All:</div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
I am hosting a special biophysics/biochemistry talk in<span class="Apple-converted-space"> </span><b>1080 (Robert Smith seminar room) Physica Research Building (PRB) at 4pm on Wednesday</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… If you really like to meet him , please let me know (he will arrive here at noon on Wednesday and leave on Thursday). Thanks. </div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
<br>
</div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
The talk title and abstract is s follows:</div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
<b class="" style="font-family: Calibri; line-height: 21px; text-align: justify;"><span class=""><br>
</span></b></div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
<b class="" style="font-family: Calibri; line-height: 21px; text-align: justify;"><span class="">Allostery in chaperonins: how and why</span></b></div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
<p class="MsoNormal" style="font-family: Calibri; text-align: justify; line-height: 21px;">
<span class="">Chaperonins </span><span class="">consist of two back-to-back stacked heptameric rings with a cavity at each end</span> where protein folding can take place. They<span class=""> 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="">two approaches </span><span class="">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> The impact of these different allosteric mechanisms on the folding functions of GroEL and CCT/TRiC will be discussed.</p>
</div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
<br>
</div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
Best regards,</div>
<div style="color: rgb(0, 0, 0); font-family: Calibri, sans-serif; font-size: 14px; font-style: normal; font-variant: normal; font-weight: normal; letter-spacing: normal; line-height: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-stroke-width: 0px;">
<br class="Apple-interchange-newline">
</div>
</span>
</body>
</html>