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<h1 style="text-align: center">NLM DIR Seminar Schedule</h1>
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<a href="/seminar/5213/detail/">March 11, 2025&nbsp;&nbsp;<b>Sofya Garushyants</b></a><br>Tmn bacterial anti-phage defense system
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<a href="/seminar/5214/detail/">March 18, 2025&nbsp;&nbsp;<b>MG Hirsch</b></a><br>TBD
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<a href="/seminar/5215/detail/">March 25, 2025&nbsp;&nbsp;<b>Yifan Yang</b></a><br>TBD
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<a href="/seminar/5216/detail/">April 1, 2025&nbsp;&nbsp;<b>Roman Kogay</b></a><br>TBD
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<a href="/seminar/5217/detail/">April 8, 2025&nbsp;&nbsp;<b>Jaya Srivastava</b></a><br>TBD
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<a href="/seminar/5212/detail/">March 4, 2025&nbsp;&nbsp;<b>Sanasar Babajanyan</b></a><br>Evolution of antivirus defense in prokaryotes depending on the environmental virus load
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<a href="/seminar/5211/detail/">Feb. 25, 2025&nbsp;&nbsp;<b>Zhizheng Wang</b></a><br>GeneAgent: Self-verification Language Agent for Gene Set Analysis using Domain Databases
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<a href="/seminar/5210/detail/">Feb. 18, 2025&nbsp;&nbsp;<b>Samuel Lee</b></a><br>Efficient predictions of alternative protein conformations by AlphaFold2-based sequence association
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<a href="/seminar/5209/detail/">Feb. 11, 2025&nbsp;&nbsp;<b>Po-Ting Lai</b></a><br>Enhancing Biomedical Relation Extraction with Directionality
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<a href="/seminar/5208/detail/">Feb. 4, 2025&nbsp;&nbsp;<b>Victor Tobiasson</b></a><br>On the dominance of Asgard contributions to Eukaryogenesis
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<h2>Scheduled Seminars on Jan. 24, 2023</h2>
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<div class="tablet:grid-col-8"><strong> Evolutionary selection of proteins with two folds </strong></div>
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<h4> Abstract: </h4>
<p><p>Although most globular proteins fold into a single stable structure, an increasing number have been shown to remodel their secondary and tertiary structures in response to cellular stimuli. State-of-the-art algorithms predict that these fold-switching proteins assume only one stable structure, missing their functionally critical alternative folds. Why these algorithms predict a single fold is unclear, but all of them infer protein structure from coevolved amino acid pairs. Here, we hypothesize that coevolutionary signatures are being missed. Suspecting that single-fold variants could be masking these signatures, we developed an approach to search both highly diverse protein superfamiliescomposed of single-fold and fold-switching variantsand protein subfamilies with more fold-switching variants. This approach successfully revealed coevolution of amino acid pairs uniquely corresponding to both conformations of 54 fold-switching proteins from distinct families. Then, using a set of coevolved amino acid pairs predicted by our approach, we successfully biased AlphaFold2 to predict two experimentally consistent conformations of a candidate protein with unsolved structure. The discovery of widespread dual-fold coevolution indicates that fold-switching sequences have been preserved by natural selection, implying that their functionalities provide evolutionary advantage and paving the way for predictions of diverse protein structures from single sequences.</p></p>
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<li><a href="/archive_seminars/2024/"><b>2024</b> Seminars</a></li>
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<li><a href="/archive_seminars/2022/"><b>2022</b> Seminars</a></li>
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<li><a href="/archive_seminars/2020/"><b>2020</b> Seminars</a></li>
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<li><a href="/archive_seminars/2017/"><b>2017</b> Seminars</a></li>
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