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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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1H-NMR and protection studies of interactions between ligands and bovine pancreatic phospholipase A2.

A number of long-chain amines and naphthylamine sulfonates have been studied for their ability to inhibit bovine pancreatic phospholipase A2 (PLA2) and to protect PLA2 against alkylation of the active site histidine by p-bromophenacyl bromide. Their areas of interaction on the enzyme were further delineated using observations of chemical shift changes of assigned aromatic signals in the 1H-NMR spectrum of PLA2, while the bound conformations of two amine inhibitors were revealed using transferred nuclear Overhauser effects. The alkyl amines bind rather non-specifically on the surface of the enzyme, over the active site cleft and the interface recognition site.[1]

References

  1. 1H-NMR and protection studies of interactions between ligands and bovine pancreatic phospholipase A2. Williamson, M.P., Davis, P.D., Broadhurst, M.J., Nixon, J.S. Biochim. Biophys. Acta (1989) [Pubmed]
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