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Default Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.

Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.

Related Articles Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins.

J Biomol NMR. 2014 Nov 9;

Authors: Guo C, Hou G, Lu X, O'Hare B, Struppe J, Polenova T

Abstract
Heteronucleus-detected dipolar based correlation spectroscopy is established for assignments of (1)H, (13)C, and (15)N resonances and structural analysis in fully protonated proteins. We demonstrate that (13)C detected 3D experiments are highly efficient and permit assignments of the majority of backbone resonances, as shown in an 89-residue dynein light chain 8, LC8 protein. With these experiments, we have resolved many ambiguities that were persistent in our previous studies using moderate MAS frequencies and lacking the (1)H dimension. The availability of (1)H isotropic chemical shifts measured with the heteronucleus-detected fast-MAS experiments presented here is essential for the accurate determination of the (1)H CSA tensors, which provide very useful structural probe. Finally, our results indicate that (13)C detection in fast-MAS HETCOR experiments may be advantageous compared with (1)H detection as it yields datasets of significantly higher resolution in the (13)C dimension than the (1)H detected HETCOR versions.


PMID: 25381566 [PubMed - as supplied by publisher]



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