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Difference between revisions of "User:Marie Sofie Moeller"
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| + | In 2013 Marie Sofie Møller completed her PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem at the Technical University of Denmark. She has mainly been focusing on structure-function relationship studies of glycoside hydrolases from family [[GH13]] <cite>Moeller2012a Moeller2012b</cite>. At the Carlsberg Research Laboratory under supervision by Anette Henriksen, she has been determining several structures of GH13_13 barley limit dextrinase including the first structure of an a-glucan debranching enzyme in complex with a natural substrate, i.e. a branched maltooligosaccharide (limit dextrin). Furthermore, she has determined the complex structure between barley limit dextrinase and its endogenous inhibitor, a 13.4 kDa cereal type inhibitor. The study of the latter complex resulted in a spin-off project, which she got granted by an individual postdoc grant from the Independent Research Fund Denmark. The project was carried out in the laboratory of Ingemar André at Lund University, Sweden. The spin-off project focused on understanding the high-affinity (pM) using computational redesign. | ||
| + | In 2016 she returned to the Technical University of Denmark, where she holds a position as Assistant Professor in the group of ^^^Birte Svensson^^^. She is currently working on a project on low affinity protein-carbohydrate interactions focusing on carbohydrate binding module families [[CBM10]] and [[CBM45]]. The CBM10s studied originate from a [[GH5]] subfamily 8 mannanase from a marine bacterium, while the CBM45s originate from a glucan, water dikinase from potato. | ||
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| − | + | #Moeller2012a pmid=22949184 | |
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| + | #Moeller2012b pmid=22685275 | ||
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Revision as of 05:02, 6 November 2019
In 2013 Marie Sofie Møller completed her PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem at the Technical University of Denmark. She has mainly been focusing on structure-function relationship studies of glycoside hydrolases from family GH13 [1, 2]. At the Carlsberg Research Laboratory under supervision by Anette Henriksen, she has been determining several structures of GH13_13 barley limit dextrinase including the first structure of an a-glucan debranching enzyme in complex with a natural substrate, i.e. a branched maltooligosaccharide (limit dextrin). Furthermore, she has determined the complex structure between barley limit dextrinase and its endogenous inhibitor, a 13.4 kDa cereal type inhibitor. The study of the latter complex resulted in a spin-off project, which she got granted by an individual postdoc grant from the Independent Research Fund Denmark. The project was carried out in the laboratory of Ingemar André at Lund University, Sweden. The spin-off project focused on understanding the high-affinity (pM) using computational redesign. In 2016 she returned to the Technical University of Denmark, where she holds a position as Assistant Professor in the group of ^^^Birte Svensson^^^. She is currently working on a project on low affinity protein-carbohydrate interactions focusing on carbohydrate binding module families CBM10 and CBM45. The CBM10s studied originate from a GH5 subfamily 8 mannanase from a marine bacterium, while the CBM45s originate from a glucan, water dikinase from potato.
- Møller MS, Abou Hachem M, Svensson B, and Henriksen A. (2012). Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012;68(Pt 9):1008-12. DOI:10.1107/S1744309112031004 |
- Møller MS, Fredslund F, Majumder A, Nakai H, Poulsen JC, Lo Leggio L, Svensson B, and Abou Hachem M. (2012). Enzymology and structure of the GH13_31 glucan 1,6-α-glucosidase that confers isomaltooligosaccharide utilization in the probiotic Lactobacillus acidophilus NCFM. J Bacteriol. 2012;194(16):4249-59. DOI:10.1128/JB.00622-12 |