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<p class="MsoNormal"><span style="color:#1F497D">Dear All,<o:p></o:p></span></p>
<p class="MsoNormal"><span style="color:#1F497D"><o:p> </o:p></span></p>
<p class="MsoNormal"><span style="color:#1F497D">Just a quick reminder of tomorrow’s seminar.<o:p></o:p></span></p>
<p class="MsoNormal"><span style="color:#1F497D"><o:p> </o:p></span></p>
<p class="MsoNormal"><span style="color:#1F497D">Cheers,<o:p></o:p></span></p>
<p class="MsoNormal"><span style="color:#1F497D">Neil<o:p></o:p></span></p>
<p class="MsoNormal"><span style="color:#1F497D"><o:p> </o:p></span></p>
<p class="MsoNormal"><span style="color:#1F497D"><o:p> </o:p></span></p>
<p class="MsoNormal"><o:p> </o:p></p>
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<b><span style="font-family:"Garamond","serif"">Visualizing fast protein dynamics: Insights from 2D IR spectroscopy and Markov state models<o:p></o:p></span></b></p>
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<b><span style="font-family:"Garamond","serif"">Weds Nov 5<sup>th</sup>, 2pm, JA 3.27<o:p></o:p></span></b></p>
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<b><span style="font-family:"Garamond","serif""><br>
</span></b><span style="font-family:"Garamond","serif"">Carlos R. Baiz</span><o:p></o:p></p>
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<span style="font-family:"Garamond","serif"">Two-dimensional infrared (2DIR) spectroscopy measures snapshots of protein conformational ensembles with subpicosecond time resolution. Amide-I vibrations, consisting of backbone C=O stretching modes, contain a wealth
of structural information, and 2D IR offers superior structural sensitivity by spreading the spectral information onto two frequency axes to measure couplings between different vibrational modes. Markov state models based on extensive molecular dynamics simulations,
offer an intuitive structural interpretation of the equilibrium ensemble and folding process that captures the diversity of folding pathways in solution. We combine these techniques to study the folding mechanism of NTL9, a 39-residue two-state á/â miniprotein,
on timescales from 100 ns to 50 ms. Simulated 2DIR spectra, generated from a Markov state model, provide a detailed view of the folding mechanism. Additionally, spectra of specific isotope-labeled residues probe hydrogen bonding environments at different points
along the protein backbone, suggesting that some secondary structures exhibit a significant degree of backbone heterogeneity and solvent exposure.</span><o:p></o:p></p>
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