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User:Eva Madland
Eva Madland has a M.Sc. in organic chemistry from the Norwegian University of Science and Technology (Trondheim, Norway), where she worked on isolation, separation and structural elucidation of natural products from plants. In 2020 she completed her PhD in Biotechnology at the Norwegian University of Science and Technology (Trondheim, Norway) under the supervision by Professor Finn Lillelund Aachmann (NTNU, Norway) and Professor Morten Sørlie (NMBU, Norway) in the Biopolymer NMR group. The work focused on studying interactions between carbohydrate-binding modules and carbohydrates using NMR spectroscopy. She is currently a postdoc in the group of Associate professor Kasper R. Andersen (Aarhus University, Denmark) where she is working on structure and function relations of receptor-mediated signalling in plant-microbe interactions.
She has worked on the following CBMs:
- CBM5 from Cellvibrio japonicus [1]
- CBM14 from human chitotriosidase [2]
- CBM73 from Cellvibrio japonicus [1]
- CBM86 from Roseburia intestinalis L1-82 [3, 4]
- Madland E, Forsberg Z, Wang Y, Lindorff-Larsen K, Niebisch A, Modregger J, Eijsink VGH, Aachmann FL, and Courtade G. (2021). Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus. J Biol Chem. 2021;297(4):101084. DOI:10.1016/j.jbc.2021.101084 |
- Madland E, Crasson O, Vandevenne M, Sørlie M, and Aachmann FL. (2019). NMR and Fluorescence Spectroscopies Reveal the Preorganized Binding Site in Family 14 Carbohydrate-Binding Module from Human Chitotriosidase. ACS Omega. 2019;4(26):21975-21984. DOI:10.1021/acsomega.9b03043 |
- Madland E, Kitaoku Y, Sætrom GI, Leth ML, Ejby M, Hachem MA, and Aachmann FL. (2019). (1)H, (13)C and (15)N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis. Biomol NMR Assign. 2019;13(1):55-58. DOI:10.1007/s12104-018-9850-3 |
- Leth ML, Ejby M, Madland E, Kitaoku Y, Slotboom DJ, Guskov A, Aachmann FL, and Abou Hachem M. (2020). Molecular insight into a new low-affinity xylan binding module from the xylanolytic gut symbiont Roseburia intestinalis. FEBS J. 2020;287(10):2105-2117. DOI:10.1111/febs.15117 |