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XB-ART-50203
Angew Chem Int Ed Engl 2015 Apr 27;5418:5328-30. doi: 10.1002/anie.201500261.
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Direct observation of Ca(2+) -induced calmodulin conformational transitions in intact Xenopus laevis oocytes by (19) F NMR spectroscopy.

Ye Y , Liu X , Xu G , Liu M , Li C .


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The Ca(2+) -mediated conformational transition of the protein calmodulin (CaM) is essential to a variety of signal transduction pathways. Whether the transition in living cells is similar to that observed in buffer is not known. Here, we report the direct observation by (19) F NMR spectroscopy of the transition of the Ca(2+) -free and -bound forms in Xenopus laevis oocytes at different Ca(2+) levels. We find that the Ca(2+) -bound CaM population increased greatly upon binding the target protein myosin light-chain kinase (MLCK) at the same Ca(2+) level. Paramagnetic NMR spectroscopy was also exploited for the first time to obtain long-range structural constraints in cells. Our study shows that (19) F NMR spectroscopy can be used to obtain long-range structural constraints in living eukaryotic cells and paves the way for quantification of protein binding constants.

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Species referenced: Xenopus laevis
Genes referenced: mylkl