Journal article
1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis
Norwegian University of Science and Technology1
Kindai University2
Department of Biotechnology and Biomedicine, Technical University of Denmark3
National Food Institute, Technical University of Denmark4
Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark5
Protein Glycoscience and Biotechnology, Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark6
The N-terminal domain (residues 28–165) from the glycoside hydrolase family 10 from Roseburia intestinalis (RiCBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli. Here we report 1H, 13C and 15N NMR chemical shift assignments for this carbohydrate binding module (CBM).
| Language: | English |
|---|---|
| Publisher: | Springer Netherlands |
| Year: | 2019 |
| Pages: | 55-58 |
| ISSN: | 1874270x and 18742718 |
| Types: | Journal article |
| DOI: | 10.1007/s12104-018-9850-3 |
| ORCIDs: | 0000-0003-1613-4663 , Leth, Maria Louise , Ejby, Morten and Abou Hachem, Maher |
Carbohydrate binding module (CBM) Gut microbiota Roseburia intestinalis Xylan binding module Xylanase
Biochemistry, general Biological and Medical Physics, Biophysics Carbon Isotopes Carbon-13 Endo-1,4-beta Xylanases Firmicutes Nitrogen Isotopes Nitrogen-15 Nuclear Magnetic Resonance, Biomolecular Physics Physics and Astronomy Polymer Sciences Protein Structure, Secondary Protons Receptors, Cell Surface saccharide-binding proteins
