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Issue 43, 2015
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Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations

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Abstract

We report a new multidimensional magic angle spinning NMR methodology, which provides an accurate and detailed probe of molecular motions occurring on timescales of nano- to microseconds, in sidechains of proteins. The approach is based on a 3D CPVC-RFDR correlation experiment recorded under fast MAS conditions (νR = 62 kHz), where 13C–1H CPVC dipolar lineshapes are recorded in a chemical shift resolved manner. The power of the technique is demonstrated in model tripeptide Tyr–(D)Ala–Phe and two nanocrystalline proteins, GB1 and LC8. We demonstrate that, through numerical simulations of dipolar lineshapes of aromatic sidechains, their detailed dynamic profile, i.e., the motional modes, is obtained. In GB1 and LC8 the results unequivocally indicate that a number of aromatic residues are dynamic, and using quantum mechanical calculations, we correlate the molecular motions of aromatic groups to their local environment in the crystal lattice. The approach presented here is general and can be readily extended to other biological systems.

Graphical abstract: Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations

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Publication details

The article was received on 29 Jul 2015, accepted on 24 Sep 2015 and first published on 25 Sep 2015


Article type: Paper
DOI: 10.1039/C5CP04475H
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Citation: Phys. Chem. Chem. Phys., 2015,17, 28789-28801
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    Analysis of local molecular motions of aromatic sidechains in proteins by 2D and 3D fast MAS NMR spectroscopy and quantum mechanical calculations

    P. Paluch, T. Pawlak, A. Jeziorna, J. Trébosc, G. Hou, A. J. Vega, J. Amoureux, M. Dracinsky, T. Polenova and M. J. Potrzebowski, Phys. Chem. Chem. Phys., 2015, 17, 28789
    DOI: 10.1039/C5CP04475H

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