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Proton assisted recoupling and protein structure determination

J. Chem. Phys. 129, 245101 (2008); doi:10.1063/1.3036928

Published 23 December 2008

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Gaël De Paëpe,1 Józef R. Lewandowski,1 Antoine Loquet,2 Anja Böckmann,2 and Robert G. Griffin1
1Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
2Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, IFR 128 BioSciences, 69367 Lyon, France
We introduce a homonuclear version of third spin assisted recoupling, a second-order mechanism that can be used for polarization transfer between 13C or 15N spins in magic angle spinning (MAS) NMR experiments, particularly at high spinning frequencies employed in contemporary high field MAS experiments. The resulting sequence, which we refer to as proton assisted recoupling (PAR), relies on a cross-term between 1H–13C (or 1H–15N) couplings to mediate zero quantum 13C–13C (or 15N–15N recoupling). In particular, using average Hamiltonian theory we derive an effective Hamiltonian for PAR and show that the transfer is mediated by trilinear terms of the form C<sub>1</sub><sup>[plus-minus]</sup>C<sub>2</sub><sup>-/+</sup>HZ for 13C–13C recoupling experiments (or N<sub>1</sub><sup>[plus-minus]</sup>N<sub>2</sub><sup>-/+</sup>HZ for 15N–15N). We use analytical and numerical simulations to explain the structure of the PAR optimization maps and to delineate the PAR matching conditions. We also detail the PAR polarization transfer dependence with respect to the local molecular geometry and explain the observed reduction in dipolar truncation. Finally, we demonstrate the utility of PAR in structural studies of proteins with 13C–13C spectra of uniformly 13C, 15N labeled microcrystalline Crh, a 85 amino acid model protein that forms a domain swapped dimer (MW=2×10.4  kDa). The spectra, which were acquired at high MAS frequencies (omegar2pi>20  kHz) and magnetic fields (750–900 MHz 1H frequencies) using moderate rf fields, exhibit numerous cross peaks corresponding to long (up to 6–7  Å) 13C–13C distances which are particularly useful in protein structure determination. Using results from PAR spectra we calculate the structure of the Crh protein. ©2008 American Institute of Physics
History: Received 12 August 2008; accepted 3 November 2008; published 23 December 2008
Permalink: http://link.aip.org/link/?JCPSA6/129/245101/1
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Supplemental Material

KEYWORDS and PACS

Keywords
PACS
  • 87.15.B-
    Structure of biomolecules
  • 02.60.-x
    Numerical approximation and analysis
  • 87.15.N-
    Properties of solutions of biological macromolecules
  • 82.56.Pp
    NMR of chemical processes in biomolecules
  • 87.14.E-
    Proteins
  • 87.80.Un
    Proteomic techniques (biophysical research methods)
  • YEAR: 2008

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ISSN:
0021-9606 (print)   1089-7690 (online)
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