@article{KramerKleinpeter2010,
  author    = {Kramer, Markus and Kleinpeter, Erich},
  title     = {STD-DOSY : a new NMR method to analyze multi-component enzyme/substrate systems},
  issn      = {1090-7807},
  doi       = {10.1016/j.jmr.2009.11.007},
  year      = {2010},
  abstract  = {A new approach to analyze multi-component Saturation Transfer Difference (STD) NMR spectra by combining the STD and the DOSY experiment is proposed. The resulting pulse sequence was successfully used to simplify an exemplary multi- component protein/substrate system by means of standard DOSY processing methods. Furthermore, the same experiment could be applied to calculate the ratio of saturated substrate molecules and its saturation rate in the case of competitive interactions. This ratio depends on the strength of this interaction between the substrates and the protein, so that this kind of information could be extracted from the results of our experiment.},
  language  = {en}
}
@article{FettkeKramerKleinpeter2010,
  author    = {Fettke, Anja and Kramer, Markus and Kleinpeter, Erich},
  title     = {Lectin-bound conformations and non-covalent interactions of glycomimetic analogs of thiochitobiose},
  issn      = {0040-4020},
  doi       = {10.1016/j.tet.2010.04.012},
  year      = {2010},
  abstract  = {The bound conformations of five S-glycoside analogs of N,N'-diacetylchitobiose as well as their non- covalent interactions with two lectins, Phytolacca americana lectin (PAL) and wheat germ agglutinin (WGA), are reported. The conformations of the ligands were examined by trNOESY experiments and compared with the free, solution-state conformations and molecular modeling data obtained by force field calculations. In the case of S-aryl, S-glycosides with exclusively S-glycosidic linkages, similar free and lectin-bound conformations and non-covalent interactions were found, whereas they differed for mixed glycosides and for a thiazoline derivative. In addition, STD (saturation transfer difference) NMR magnetization transfer efficiencies at three different temperatures were determined and assessed with respect to the structural differences of these pseudosaccharides. The binding epitopes of each substrate with PAL and WGA were also determined.},
  language  = {en}
}