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Spin Labels as a Tool to Identify and Characterize Protein–Ligand Interactions by NMR Spectroscopy
Author(s) -
Jahnke Wolfgang
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020301)3:2/3<167::aid-cbic167>3.0.co;2-s
Subject(s) - nuclear magnetic resonance spectroscopy , drug discovery , nitroxide mediated radical polymerization , linker , spectroscopy , chemistry , robustness (evolution) , site directed spin labeling , transverse relaxation optimized spectroscopy , two dimensional nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , fluorine 19 nmr , combinatorial chemistry , chemical physics , computational chemistry , stereochemistry , computer science , organic chemistry , electron paramagnetic resonance , polymer , physics , monomer , biochemistry , radical polymerization , quantum mechanics , gene , operating system
NMR spectroscopy based discovery and optimization of lead compounds for a given molecular target requires the development of methods with maximum sensitivity and robustness. It is shown here that organic nitroxide radicals (“spin labels”) can be used to boost the sensitivity of NMR spectroscopic screening in drug discovery research. The concept of utilizing spin labels in NMR spectroscopy is summarized, examples for successful first‐site and second‐site NMR spectroscopic screens are given, and guidelines for linker design are presented.