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<p class="MsoNormal"><span style="font-size:15.0pt">There will be a <b><span style="color:red">virtual</span></b><span style="color:red">
</span>Modern Optics and Spectroscopy Seminar held <b>tomorrow, November 30 at 12pm.
</b>A short Q&A segment will immediately follow the conclusion of the seminar.</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt"> </span><o:p></o:p></p>
<p class="MsoNormal"><b><i><span style="font-size:15.0pt">Zoom link:<span style="color:red">
<a href="https://mit.zoom.us/j/95781758126?pwd=ZGgxbnF5ZFZwOU9BNnFubDcyNWw1Zz09">
<span style="color:red">https://mit.zoom.us/j/95781758126?pwd=ZGgxbnF5ZFZwOU9BNnFubDcyNWw1Zz09</span></a></span><br>
</span></i></b><b><span style="font-size:16.0pt">Password: <span style="color:red">
729315</span></span></b><o:p></o:p></p>
<p class="MsoNormal"><b><span style="font-size:15.0pt">__________________________</span></b><o:p></o:p></p>
<p class="MsoNormal"><b><span style="font-size:18.0pt"><br>
Ben Schuler<br>
</span></b><b><span style="font-size:17.0pt">University of Zurich (Switzerland)</span></b><i><span style="font-size:14.0pt"><br>
<br>
</span></i><b><i><span style="font-size:16.0pt">“Probing the Dynamics and Interaction Mechanisms of
<br>
Intrinsically Disordered Proteins with Single-Molecule Spectroscopy”</span></i></b><o:p></o:p></p>
<p class="MsoNormal"><i><br>
The functions of proteins have traditionally been linked to their well-defined three-dimensional, folded structures. It is now clear, however, that many proteins perform essential functions without being folded. Quantifying the highly dynamic and conformationally
diverse ensembles of such unfolded or ‘intrinsically disordered’ proteins (IDPs) is an important aspect of understanding their functional mechanisms. Single-molecule spectroscopy is ideally suited for investigating these systems. I will illustrate how the
combination of single-molecule Förster resonance energy transfer (FRET) with nanosecond correlation spectroscopy, microfluidic mixing, and other methods can be used to probe the intra- and intermolecular distance distributions, reconfiguration dynamics, and
interactions over a wide range of timescales, and in heterogeneous environments, including live cells.<br>
<br>
_____________________</i><i><span style="font-size:11.0pt"><br>
</span></i> <o:p></o:p></p>
<p class="MsoNormal"><b><span style="font-size:11.0pt">Christine Brooks</span></b><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">Administrative Assistant</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">Massachusetts Institute of Technology</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">Department of Chemistry</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">77 Massachusetts Ave, 6-333</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">Cambridge, MA 02139</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">p: 617.253.7239</span><o:p></o:p></p>
<p class="MsoNormal"><span style="font-size:11.0pt">e: <a href="mailto:cbrooks@mit.edu">cbrooks@mit.edu</a></span><o:p></o:p></p>
<p class="MsoNormal"> <o:p></o:p></p>
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