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Two‐dimensional 1 H NMR studies of Ca(II)‐binding site in proteins using paramagnetic lanthanides(III) as probes and Yb(III)‐substituted bovine α‐lactalbumin as an example
Author(s) -
Ming Lijune
Publication year - 1993
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260311320
Subject(s) - chemistry , lanthanide , nmr spectra database , moiety , two dimensional nuclear magnetic resonance spectroscopy , paramagnetism , spectral line , crystallography , proton nmr , nuclear magnetic resonance spectroscopy , stereochemistry , metal , ion , organic chemistry , physics , quantum mechanics , astronomy
Substitution of Yb 3+ for the Ca 2+ in bovine α‐lactalbumin affords a derivative that gives rise to several isotropically shifted 1 H NMR signals in the range 80 to − 35 ppm in D 2 O. Despite the broadness of the isotropically shifted features, cross signals in both NOESY and COSY spectra have been detected. Several Asp residues in the metal‐binding loop can be recognized in the 2D 1 H NMR spectra of this derivative, showing cross signals among the protons of a C β H 2 C α H moiety. This paper reports 2D 1 H NMR studies of a paramagnetic lanthanide(III)‐substituted Ca 2+ −containing protein that may serve as a model for future NMR studies of other biochemically significant Ca 2+ proteins.