@article{LandstroemNordmarkEklundetal.2008,
  author    = {Landstr{\"o}m, Jens and Nordmark, Eva-Lisa and Eklund, Robert and Weintraub, Andrej and Seckler, Robert and Widmalm, G{\"o}ran},
  title     = {Interaction of a Salmonella enteritidis O-antigen octasaccharide with the phage P22 tailspike protein by NMR spectroscopy and docking studies},
  issn      = {0282-0080},
  doi       = {10.1007/s10719-007-9065-9},
  year      = {2008},
  abstract  = {The tailspike protein P22 recognizes an octasaccharide derived from the O-antigen polysaccharide of Salmonella enteritidis in a shallow groove and molecular docking successfully identifies this binding region on the protein surface. Analysis by 2D 1H,1H-T-ROESY and transferred NOESY NMR experiments indicate that the bound octasaccharide ligand has a conformation similar to that observed in solution. The results from a saturation transfer difference NMR experiment show that a large number of protons in the octasaccharide are in close contact with the protein as a result of binding. A comparison of the crystal structure of the complex and a molecular dynamics simulation of the octasaccharide with explicit water molecules suggest that only minor conformational changes are needed upon binding to the tailspike protein.},
  language  = {en}
}