Smaller amounts of proteins are now required to screen for weak binding interactions between ligands and the active site of metalloproteins as a result of the substitution of diamagnetic zinc(II) with paramagnetic cobalt(II) in the matrix metalloproteinase MMP-12. 1H NMR spectroscopy then provides qualitative information on the orientation of the ligand in the catalytic site targeted by drugs (see picture).
Paramagnetic metal ions in ligand screening: The Co-II matrix metalloproteinase 12 / I. Bertini; M. Fragai; Y. M. Lee; C. Luchinat; B. Terni. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 43:(2004), pp. 2254-2256. [10.1002/anie.200353453]
Paramagnetic metal ions in ligand screening: The Co-II matrix metalloproteinase 12
BERTINI, IVANO;FRAGAI, MARCO;LEE, YONG-MIN;LUCHINAT, CLAUDIO;TERNI, BEATRICE
2004
Abstract
Smaller amounts of proteins are now required to screen for weak binding interactions between ligands and the active site of metalloproteins as a result of the substitution of diamagnetic zinc(II) with paramagnetic cobalt(II) in the matrix metalloproteinase MMP-12. 1H NMR spectroscopy then provides qualitative information on the orientation of the ligand in the catalytic site targeted by drugs (see picture).File | Dimensione | Formato | |
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