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Interdomain Dynamics Explored by Paramagnetic NMR

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Interdomain Dynamics Explored by Paramagnetic NMR

NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11 37077 Göttingen, Germany
J. Am. Chem. Soc., 2013, 135 (45), pp 17111–17120
DOI: 10.1021/ja408143f
Publication Date (Web): October 11, 2013
Copyright © 2013 American Chemical Society


Abstract Image

An ensemble-based approach is presented to explore the conformational space sampled by a multidomain protein showing moderate interdomain dynamics in terms of translational and rotational motions. The strategy was applied on a complex of calmodulin (CaM) with the IQ-recognition motif from the voltage-gated calcium channel Cav1.2 (IQ), which adopts three different interdomain orientations in the crystal. The N60D mutant of calmodulin was used to collect pseudocontact shifts and paramagnetically induced residual dipolar couplings for six different lanthanide ions. Then, starting from the crystal structure, pools of conformations were generated by free MD. We found the three crystal conformations in solution, but four additional MD-derived conformations had to be included into the ensemble to fulfill all the paramagnetic data and cross-validate optimally against unused paramagnetic data. Alternative approaches led to similar ensembles. Our “ensemble” approach is a simple and efficient tool to probe and describe the interdomain dynamics and represents a general method that can be used to provide a proper ensemble description of multidomain proteins.


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  • Published In Issue November 13, 2013
  • Article ASAPNovember 04, 2013
  • Just Accepted ManuscriptOctober 11, 2013
  • Received: August 06, 2013

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