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  Interdomain dynamics explored by paramagnetic NMR.

Russo, L., Maestre Martinez, M., Wolff, S., Becker, S., & Griesinger, C. (2013). Interdomain dynamics explored by paramagnetic NMR. Journal of the American Chemical Society, 135(45), 17111-17120. doi:10.1021/ja408143f.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-CE01-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-3B05-D
Genre: Journal Article

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http://pubs.acs.org/doi/pdf/10.1021/ja408143f (Publisher version)
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 Creators:
Russo, L.1, Author              
Maestre Martinez, M.1, Author              
Wolff, S.1, Author              
Becker, S.1, Author              
Griesinger, C.1, Author              
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: 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 (CalvI) with the IQ:recognition motif from the voltage-gated calcium channel Ca(v)1.2 (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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Language(s): eng - English
 Dates: 2013-11-13
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/ja408143f
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 135 (45) Sequence Number: - Start / End Page: 17111 - 17120 Identifier: -