This work was performed in the Center of Biological NMR, the Hong Kong University of Science and Technology and was supported in part by grants to G.Z. from the Research Grants Council of Hong Kong (6199/99M and 6208/00M) and to D.L. from the National Natural Science Foundation of China (19975038).
机构署名：
本校为其他机构
院系归属：
化学学院
摘要：
The interaction of Ca2+-free calmodulin (apoCaM) with the IQ motif corresponding to the calmodulin-binding domain of neurogranin has been studied by nuclear magnetic resonance (NMR) methods. The NMR spectra of uncomplexed apoCaM and apoCaM in complex with the IQ motif recorded at 750MHz were studied and the backbone assignments of the protein in both forms were obtained by triple-resonance multidimensional NMR experiments. Chemical shift perturbations were used to map the binding surfaces. Only a single set of resonances was observed throughout...
