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Generation of Pseudocontact Shifts in Protein NMR Spectra with a Genetically Encoded Cobalt(II)‐Binding Amino Acid
Author(s) -
Nguyen Thi Hoang Duong,
Ozawa Kiyoshi,
StantonCook Mitchell,
Barrow Russell,
Huber Thomas,
Otting Gottfried
Publication year - 2011
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.201005672
Subject(s) - amino acid , computational biology , representation (politics) , nmr spectra database , chemistry , ligand (biochemistry) , cobalt , biochemistry , spectral line , biology , physics , inorganic chemistry , receptor , astronomy , politics , political science , law
Playing tag : Incorporation of the genetically encoded amino acid bipyridylalanine into a protein creates a site‐specific binding site for Co II . Pronounced pseudocontact shifts generated by the Co II ion in the NMR spectra delivers powerful long‐range structure information for the facile analysis of proteins as well as protein–protein and protein–ligand complexes (see picture for a representation of the psuedocontact shift in the protein).