Paëpe, Gaël De, Lewandowski, Józef R., Loquet, Antoine, Eddy, Matt, Megy, Simon, Böckmann, Anja and Griffin, Robert G. (2011) Heteronuclear proton assisted recoupling. The Journal of Chemical Physics, Vol.134 (No.9). 095101. doi:10.1063/1.3541251 ISSN 0021-9606.

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Abstract

We describe a theoretical framework for understanding the heteronuclear version of the third spin assisted recoupling polarization transfer mechanism and demonstrate its potential for detecting long-distance intramolecular and intermolecular (15)N-(13)C contacts in biomolecular systems. The pulse sequence, proton assisted insensitive nuclei cross polarization (PAIN-CP) relies on a cross term between (1)H-(15)N and (1)H-(13)C dipolar couplings to mediate zero-and/or double-quantum (15)N-(13)C recoupling. In particular, using average Hamiltonian theory we derive effective Hamiltonians for PAIN-CP and show that the transfer is mediated by trilinear terms of the form N(+/-)C(-/+)H(z) (ZQ) or N(+/-)C(-/+)H(z) (DQ) depending on the rf field strengths employed. We use analytical and numerical simulations to explain the structure of the PAIN-CP optimization maps and to delineate the appropriate matching conditions. We also detail the dependence of the PAIN-CP polarization transfer with respect to local molecular geometry and explain the observed reduction in dipolar truncation. In addition, we demonstrate the utility of PAIN-CP in structural studies with (15)N-(13)C spectra of two uniformly (13)C, (15)N labeled model microcrystalline proteins-GB1, a 56 amino acid peptide, and Crh, a 85 amino acid domain swapped dimer (MW = 2 x 10.4 kDa). The spectra acquired at high magic angle spinning frequencies (omega(r)/2 pi > 20 kHz) and magnetic fields (omega(0H)/2 pi = 700-900 MHz) using moderate rf fields, yield multiple long-distance intramonomer and intermonomer (15)N-(13)C contacts. We use these distance restraints, in combination with the available x-ray structure as a homology model, to perform a calculation of the monomer subunit of the Crh protein. (C) 2011 American Institute of Physics. [doi: 10.1063/1.3541251]

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Divisions:	Faculty of Science, Engineering and Medicine > Science > Chemistry
Library of Congress Subject Headings (LCSH):	Nuclear magnetic resonance spectroscopy, Irradiation -- Physiological effect, Hamiltonian systems, Proteins
Journal or Publication Title:	The Journal of Chemical Physics
Publisher:	American Institute of Physics
ISSN:	0021-9606
Official Date:	7 March 2011
Dates:	Date Event 7 March 2011 Published
Volume:	Vol.134
Number:	No.9
Page Range:	095101
DOI:	10.1063/1.3541251
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	National Institutes of Health (U.S.) (NIH), France. Agence nationale de la recherche (ANR), European Union (EU), Sixth Framework Programme (European Commission) (FP6)
Grant number:	EB-003151 (NIH), EB-002026 (NIH), ANR08-CEXC-003-01 (ANR), JC05_44957 (ANR), PIEF-GA-2009-237646 (EU), PIRG03-GA-2008-231026 (EU), RII3-026145 (FP6)

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