392 lines
44 KiB
HTML
392 lines
44 KiB
HTML
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<meta name="title" property="og:title" content="Stadtman Tenure Track Investigator, NLM DIR">
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<title>NLM Intramural Research Program - Lauren Porter, PhD</title>
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<meta name="DC.Date.Issued" content="2020-02-13" />
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<h1 class="forstaffpages" style="opacity: 1;">Lauren Porter, PhD</h1>
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<h2>About</h2>
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<img src="https://www.nlm.nih.gov/research/img/laurenporter.jpg" alt="Picture of Lauren Porter, PhD"/>
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<h3>Lauren Porter, PhD</h3>
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Stadtman Tenure Track Investigator, NLM DIR
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<p>Dr. Porter’s lab researches fold-switching proteins, a recently discovered class of proteins that can change their structures and functions in response to changes in their environments.</p>
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<p><a href="/research/researchstaff/labs/porter" style="color: white;">Laboratory</a></p>
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<h3>Contact Information</h3>
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<p>Building 38A, 8600 Rockville Pike, Bethesda, MD 20894</p>
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<p>Tel: 301-827-0924</p>
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<p><a href="mailto:lauren.porter@nih.gov">lauren.porter@nih.gov</a></p>
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<h2>Research Interests</h2>
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<p><iframe src="https://www.youtube.com/embed/IeX5ebadgiA" allow="accelerometer; autoplay; clipboard-write; encrypted-media; gyroscope; picture-in-picture" allowfullscreen="" width="709" height="399" frameborder="0"></iframe><p>
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<p>No introductory-level biochemistry textbook is complete without a chapter about how a protein’s primary sequence of amino acids determines its fold. Despite much technical progress, however, solving protein structures experimentally remains very laborious and expensive, and knowing the structures of diverse proteins is crucial for both basic research and drug design. Thus, computational prediction of a protein’s structure from its amino acid sequence is a challenge of major importance.</p>
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<p>Nearly all computational work so far has focused on predicting a single protein structure from the protein’s amino acid sequence. Dr. Porter’s research challenges the one-sequence-one-structure paradigm. In a recent publication, Loren Looger and she found nearly 100 examples of proteins that can adopt more than one stable fold. This structural heterogeneity allows proteins either to perform more than one function or to be highly regulated in cells. Through the NLM Division of Intramural Research, her lab is developing data-driven computational approaches to predict which amino acid sequences can switch folds. She and her lab members validate these predictions experimentally at the National Heart, Lung, and Blood Institute (NHLBI).</p>
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<p>This basic research has significant implications for human health. A number of fold-switching proteins are associated with diseases such as cancer, autoimmune disorders, and bacterial and viral infections. Right now, very little is known about how these proteins work. Understanding their mechanisms could lead to development of new therapeutics.</p>
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<h2>Biography</h2>
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<p>Dr. Lauren Porter is a Stadtman Tenure-track Investigator with a primary appointment at NLM and a secondary appointment at NHLBI. Prior to coming to the NIH, Dr. Porter spent 7 years studying the biological and biophysical properties of fold-switching proteins, first at the University of Maryland and then at the Howard Hughes Medical Institute, Janelia Research Campus. She is the corresponding author of several recent papers reporting the results of this research. One of them, published in PNAS, was highlighted by two members of Faculty of 1000. For her research on protein fold switching, Dr. Porter has received the Maryland Academy of Science’s Outstanding Young Scientist Award (2015) and a National Research Service Award (2014), and she has presented her research at nearly 20 national and international conferences.</p>
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<h2>Publications</h2>
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Schafer JW, Porter LL.
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</span><a href="https://www.ncbi.nlm.nih.gov/pubmed/37673981/">
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Evolutionary selection of proteins with two folds.
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</a><span class="source">Nat Commun</span>.
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<span class="pubdate">2023 Sep 6;</span><span class="volume">14</span><span class="issue">(1)</span><span class="pages">:5478</span><span>. </span><span class="doi">doi: 10.1038/s41467-023-41237-2. </span><span class="pmid">PubMed PMID:
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37673981</span><span class="pmcid">; PubMed Central PMCID:
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PMC10482954</span><span>. </span>
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Porter LL.
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</span><a href="https://www.ncbi.nlm.nih.gov/pubmed/37431685/">
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Fluid protein fold space and its implications.
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</a><span class="source">Bioessays</span>.
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<span class="pubdate">2023 Sep;</span><span class="volume">45</span><span class="issue">(9)</span><span class="pages">:e2300057</span><span>. </span><span class="doi">doi: 10.1002/bies.202300057. </span><span class="pubstatus">Epub 2023 Jul 11. </span><span class="pmid">PubMed PMID:
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37431685</span><span class="pmcid">; PubMed Central PMCID:
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PMC10529699</span><span>. </span>
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<span class="authors">
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Chakravarty D, Sreenivasan S, Swint-Kruse L, Porter LL.
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</span><a href="https://www.ncbi.nlm.nih.gov/pubmed/37264049/">
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Identification of a covert evolutionary pathway between two protein folds.
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</a><span class="source">Nat Commun</span>.
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<span class="pubdate">2023 Jun 1;</span><span class="volume">14</span><span class="issue">(1)</span><span class="pages">:3177</span><span>. </span><span class="doi">doi: 10.1038/s41467-023-38519-0. </span><span class="pmid">PubMed PMID:
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37264049</span><span class="pmcid">; PubMed Central PMCID:
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PMC10235069</span><span>. </span>
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<div class="ncbi-docsum">
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<span class="authors">
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Aponte Santiago N, Konecki S, Porter L, Virk H.
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</span><a href="https://www.ncbi.nlm.nih.gov/pubmed/37013952/">
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Tales of the unexpected.
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</a><span class="source">Elife</span>.
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<span class="pubdate">2023 Apr 4;</span><span class="volume">12</span><span>. </span><span class="doi">doi: 10.7554/eLife.87444. </span><span class="pmid">PubMed PMID:
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<h3><a href="https://www.ncbi.nlm.nih.gov/myncbi/lauren.porter.1/bibliography/public/">More</a></h3>
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