User:Christopher Berndsen/Labinfo

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==The Berndsen Laboratory at James Madison University==
==The Berndsen Laboratory at James Madison University==
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The Berndsen Lab is located in the [http://www.jmu.edu/chemistry/ Department of Chemistry and Biochemistry] at [http://www.jmu.edu James Madison University] in Harrisonburg, VA. The primary research focus is the mechanism enzymes involved in the conjugation and processing of ubiquitin and ubiquitin-like proteins.
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The Berndsen Lab is located in the [http://www.jmu.edu/chemistry/ Department of Chemistry and Biochemistry] at [http://www.jmu.edu James Madison University] in Harrisonburg, VA. The primary research focus is the mechanism enzymes involved in the conjugation and processing of ubiquitin and ubiquitin-like proteins. Additionally, the lab is interested in integrating protein structure research and molecular basis for disease into the biochemistry classroom.
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== Function ==
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== Research Highlights ==
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Ubiquitin and Ubiquitin-like proteins are linked to many cellular functions included protein degradation and DNA damage repair <ref>PMID:15571809<ref><ref>PMID:24699078<ref>. The Berndsen Lab is interested in the catalytic mechanisms the conjugating enzymes E1, E2, and E3 use to attach ubiquitin/ubiquitin-like proteins to the substrate lysine. We are also interested in the proteases that remove these modifications and the chemical mechanism(s) of catalysis. We are currently focusing on UFM1<Structure load='1WXS' size='350' frame='true' align='right' caption='NMR Structure of UFM1 from <ref>PMID:16527251<ref>' scene='UFM1' />
== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
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== References ==
== References ==
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<references/>

Revision as of 19:39, 1 March 2016

The Berndsen Laboratory at James Madison University

Caption for this structure

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References

  1. PMID:15571809<ref><ref>PMID:24699078<ref>. The Berndsen Lab is interested in the catalytic mechanisms the conjugating enzymes E1, E2, and E3 use to attach ubiquitin/ubiquitin-like proteins to the substrate lysine. We are also interested in the proteases that remove these modifications and the chemical mechanism(s) of catalysis. We are currently focusing on UFM1<Structure load='1WXS' size='350' frame='true' align='right' caption='NMR Structure of UFM1 from <ref>PMID:16527251<ref>' scene='UFM1' /> == Disease == == Relevance == == Structural highlights == </li></ol></ref>

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Christopher Berndsen

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