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Paramagnetic NMR study of Cu 2+ –IDA complex localization on a protein surface and its application to elucidate long distance information
Author(s) -
Nomura Makoto,
Kobayashi Toshitatsu,
Kohno Toshiyuki,
Fujiwara Kenichiro,
Tenno Takeshi,
Shirakawa Masahiro,
Ishizaki Itsuko,
Yamamoto Kazuo,
Matsuyama Toshifumi,
Mishima Masaki,
Kojima Chojiro
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.04.023
Subject(s) - paramagnetism , chemistry , crystallography , histidine , iminodiacetic acid , amide , relaxation (psychology) , nuclear magnetic resonance , chelation , inorganic chemistry , amino acid , biochemistry , social psychology , psychology , physics , quantum mechanics
The paramagnetic metal chelate complex Cu 2+ ‐iminodiacetic acid (Cu 2+ –IDA) was mixed with ubiquitin, a small globular protein. Quantitative analyses of 1 H and 15 N chemical shift changes and line broadenings induced by the paramagnetic effects indicated that Cu 2+ –IDA was localized to a histidine residue (His68) on the ubiquitin surface. The distances between the backbone amide proton and the Cu 2+ relaxation center were evaluated from the proton transverse relaxation rates enhanced by the paramagnetic effect. These correlated well with the distances calculated from the crystal structure up to 20 Å. Here, we show that a Cu 2+ –IDA is the first paramagnetic reagent that specifically localizes to a histidine residue on the protein surface and gives the long‐range distance information.