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Difference between revisions of "User:Margrethe Gaardlos"

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'''This is an empty template to help you get started with composing your User page.'''
 
  
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Margrethe Gaardløs obtained her M.Sc. in Biotechnology at the Norwegian University of Life Sciences in 2015, working on biochemical characterization of lytic polysaccharide monooxygenases. She obtained a PhD in Biotechnology at the Norwegian University of Science and Technology in Trondheim, Norway, supervised by Professor [[User:Finn Aachmann|Finn Aachmann]] and co-supervised by [[User:Anne Tondervik|Anne Tondervik]]. During her PhD she studied the alginate epimerases produced by ''Azotobacter vinelandii''. The work focused on understanding the enzyme-substrate interactions, mechanism and mode of action of these enzymes through mutational studies and biochemical and biophysical analysis (<cite>stanisci2020</cite>, <cite>gaardlos2021a</cite>, <cite>gaardlos2021b</cite>). She is currently a postdoctoral researcher in the group of Sergey Samsonov at University of Gdańsk, Poland, where she works with computational modeling of glycosaminoglycans, various proteins, and their interactions.      
  
* See [[User:Gerlind_Sulzenbacher]] for an example.  You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.
 
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#stanisci2020 pmid=32149266
  
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#gaardlos2021a pmid=33822050
  
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#gaardlos2021b pmid=34878812
 
 
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#Gilbert2008 pmid=18430603
 
  
 
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Latest revision as of 10:36, 3 January 2022

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Margrethe Gaardløs obtained her M.Sc. in Biotechnology at the Norwegian University of Life Sciences in 2015, working on biochemical characterization of lytic polysaccharide monooxygenases. She obtained a PhD in Biotechnology at the Norwegian University of Science and Technology in Trondheim, Norway, supervised by Professor Finn Aachmann and co-supervised by Anne Tondervik. During her PhD she studied the alginate epimerases produced by Azotobacter vinelandii. The work focused on understanding the enzyme-substrate interactions, mechanism and mode of action of these enzymes through mutational studies and biochemical and biophysical analysis ([1], [2], [3]). She is currently a postdoctoral researcher in the group of Sergey Samsonov at University of Gdańsk, Poland, where she works with computational modeling of glycosaminoglycans, various proteins, and their interactions.



  1. Stanisci A, Tøndervik A, Gaardløs M, Lervik A, Skjåk-Bræk G, Sletta H, and Aachmann FL. (2020). Identification of a Pivotal Residue for Determining the Block Structure-Forming Properties of Alginate C-5 Epimerases. ACS Omega. 2020;5(8):4352-4361. DOI:10.1021/acsomega.9b04490 | PubMed ID:32149266 [stanisci2020]
  2. Gaardløs M, Samsonov SA, Sletmoen M, Hjørnevik M, Sætrom GI, Tøndervik A, and Aachmann FL. (2021). Insights into the roles of charged residues in substrate binding and mode of action of mannuronan C-5 epimerase AlgE4. Glycobiology. 2021;31(12):1616-1635. DOI:10.1093/glycob/cwab025 | PubMed ID:33822050 [gaardlos2021a]
  3. Gaardløs M, Heggeset TMB, Tøndervik A, Tezé D, Svensson B, Ertesvåg H, Sletta H, and Aachmann FL. (2022). Mechanistic Basis for Understanding the Dual Activities of the Bifunctional Azotobacter vinelandii Mannuronan C-5-Epimerase and Alginate Lyase AlgE7. Appl Environ Microbiol. 2022;88(3):e0183621. DOI:10.1128/AEM.01836-21 | PubMed ID:34878812 [gaardlos2021b]

All Medline abstracts: PubMed