This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. It is well established that tryptophan lines the VDR binding pocket and is positioned parallell to intercyclic 5,7-diene vitamin moieties. Since double bonds usually shield protons positioned under them, we expect that chemical shifts of tryptophan nuclei could be dependent on the orientation of vitamin D double bonds. Two tryptophan nitrogen atoms: backbone and side chain create hydrogen bonds with solvent and neighboring amino acids. These interactions can influence NMR spectra by causing signal line broadening and by changing chemical shifts. The above, combined with the fact that only one Trp molecule is present in VDR, motivated us to choose this amino acid as a convenient probe to determine binding sites in vitamin D-VDR complexes.
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