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An Accurate Pharmacophore Mapping Method by NMR Spectroscopy
Author(s) -
Mizukoshi Yumiko,
Abe Aya,
Takizawa Takeshi,
Hanzawa Hiroyuki,
Fukunishi Yoshifumi,
Shimada Ichio,
Takahashi Hideo
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201104905
Subject(s) - pharmacophore , ligand (biochemistry) , inversion (geology) , saturation (graph theory) , significant difference , chemistry , irradiation , information retrieval , computer science , crystallography , nuclear magnetic resonance , physics , stereochemistry , mathematics , nuclear physics , biochemistry , biology , combinatorics , statistics , paleontology , receptor , structural basin
Irradiation makes the difference : The relaxation‐rate differences of individual ligand protons (H A , H B ) between the experiment with (see picture, red) and that without (blue) saturation of the protons of the protein target reflect the proximity to the protein surface. Thus, the binding portions of ligand molecules could be identified using this “ d ifference of i nversion rec overy rate with and without t arget i rradiati on ” (DIRECTION) method.