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_config.yml

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details_dir: bibliography
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details_link: Details
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query: "@*"
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group_by: year
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group_order: descending
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# query: "@*"
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# group_by: year
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# group_order: descending
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# Display different badges withs stats for your publications
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# Customize badge behavior in _layouts/bib.liquid

_pages/about.md

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<!-- Introduce about the Lab -->
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# Welcome to the O'Brien Lab
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The **O'Brien Lab** at Penn State University is at the forefront of **Physical Bioinformatics** research, combining computational modeling, molecular dynamics simulations, and experimental approaches to understand the fundamental mechanisms of protein synthesis and folding in living cells.
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The O'Brien Lab at Penn State University is at the forefront of Physical Bioinformatics research, combining computational modeling, molecular dynamics simulations, and experimental approaches to understand the fundamental mechanisms of protein synthesis and folding in living cells.
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## Our Research Mission
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We develop and apply cutting-edge **Physical Bioinformatic techniques** to measure rates of translation transcriptome-wide and understand their molecular origins as they relate to fundamental biology and disease. Our work bridges the gap between computational physics and molecular biology, providing insights into how proteins achieve their functional conformations during synthesis.
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We develop and apply cutting-edge Physical Bioinformatic techniques to measure rates of translation transcriptome-wide and understand their molecular origins as they relate to fundamental biology and disease. Our work bridges the gap between computational physics and molecular biology, providing insights into how proteins achieve their functional conformations during synthesis.
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The O'Brien Lab is part of the **Department of Chemistry** and the **Institute for Computational and Data Sciences** at Penn State University, providing a unique interdisciplinary environment for cutting-edge research at the interface of physics, chemistry, and biology.
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The O'Brien Lab is part of the Department of Chemistry and the Institute for Computational and Data Sciences at Penn State University, providing a unique interdisciplinary environment for cutting-edge research at the interface of physics, chemistry, and biology.

_pages/join_us.md

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The **O'Brien Lab** at Penn State University is seeking talented individuals to join our research team. We welcome both **experimental** and **computational** candidates at the **graduate** and **postdoc** levels.
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The O'Brien Lab at Penn State University is seeking talented individuals to join our research team. We welcome both experimental and computational candidates at the graduate and postdoc levels.
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## **Open Positions**
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_pages/publications.md

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{% include bib_search.liquid %}
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<div class="publications">
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{% bibliography %}
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</div>
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{% bibliography %}
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<style>
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.publications {
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counter-reset: publication-counter;
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}
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</div>
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.publications .title {
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counter-increment: publication-counter;
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}
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.publications .title::before {
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content: counter(publication-counter) ". ";
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font-weight: bold;
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}
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</style>

_pages/research.md

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We investigate how proteins begin folding while they are still being synthesized by the ribosome. Our research has revealed that the rate at which individual amino acids are incorporated during translation can dramatically affect protein folding outcomes, potentially leading to misfolding and disease.
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##### **Translation Elongation Kinetics**
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Using advanced computational methods and ribosome profiling data, we study how translation speed varies along mRNA sequences and how this affects protein behavior. Our lab has developed innovative tools like **RiboA** for accurate analysis of ribosome profiling data.
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Using advanced computational methods and ribosome profiling data, we study how translation speed varies along mRNA sequences and how this affects protein behavior. Our lab has developed innovative tools like RiboA for accurate analysis of ribosome profiling data.
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##### **Mechanochemistry in Translation**
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We explore how mechanical forces generated during protein synthesis can feed back to influence translation rates. Our work has uncovered how charged amino acid sequences can create forces that alter the ribosome's catalytic cycle.
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##### **Protein Misfolding and Disease**
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We investigate novel mechanisms of protein misfolding, including **non-covalent lasso entanglements**, and explore therapeutic strategies to prevent misfolding-related diseases. Our recent work has shown how small molecules might be designed to prevent specific types of misfolding.
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We investigate novel mechanisms of protein misfolding, including non-covalent lasso entanglements, and explore therapeutic strategies to prevent misfolding-related diseases. Our recent work has shown how small molecules might be designed to prevent specific types of misfolding.
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##### **Computational Method Development**
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We develop theoretical frameworks and computational tools to predict and understand co-translational processes. Our approaches include:

_pages/team.md

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image: nissley.jpg
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content: team/alumni/about_Dan_Nissley.md
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image_circular: true
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more_info: >

assets/img/nissley.jpg

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