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Heteronuclear proton assisted recoupling

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dc.contributor.author Paepe, Gael De
dc.contributor.author Lewandowski, Jozef R.
dc.contributor.author Loquet, Antoine
dc.contributor.author Eddy, Matthew Thomas
dc.contributor.author Megy, Simon
dc.contributor.author Bockmann, Anja
dc.contributor.author Griffin, Robert Guy
dc.date.accessioned 2012-11-01T19:33:00Z
dc.date.available 2012-11-01T19:33:00Z
dc.date.issued 2011-03
dc.date.submitted 2010-10
dc.identifier.issn 0021-9606
dc.identifier.issn 1089-7690
dc.identifier.uri http://hdl.handle.net/1721.1/74555
dc.description.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 [superscript 15]N–[superscript 13]C contacts in biomolecular systems. The pulse sequence, proton assisted insensitive nuclei cross polarization (PAIN-CP) relies on a cross term between [superscript 1]H–[superscript 15]N and [superscript 1]H–[superscript 13]C dipolar couplings to mediate zero- and/or double-quantum [superscript 15]N–[superscript 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∓Hz (ZQ) or N±C±Hz (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 [superscript 15]N–[superscript 13]C spectra of two uniformly [superscript 13]C,[superscript 15]N labeled model microcrystalline proteins—GB1, a 56 amino acid peptide, and Crh, a 85 amino acid domain swapped dimer (MW = 2 × 10.4 kDa). The spectra acquired at high magic angle spinning frequencies (ω[subscript r]/2π > 20 kHz) and magnetic fields (ω[subscript 0H]/2π = 700–900 MHz) using moderate rf fields, yield multiple long-distance intramonomer and intermonomer [superscript 15]N–[superscript 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. en_US
dc.description.sponsorship National Institutes of Health (U.S.) (Grant EB-003151) en_US
dc.description.sponsorship National Institutes of Health (U.S.) (Grant EB-002026) en_US
dc.description.sponsorship French National Research Agency (ANR) (ANR08-CEXC-003-01) en_US
dc.description.sponsorship French National Research Agency (ANR) (JC05_44957) en_US
dc.description.sponsorship Marie Curie International Fellowship (PIEF-GA- 2009-237646) en_US
dc.description.sponsorship Marie Curie International Reintegration Grants (PIRG03-GA-2008-231026) en_US
dc.language.iso en_US
dc.publisher American Institute of Physics (AIP) en_US
dc.relation.isversionof http://dx.doi.org/ 10.1063/1.3541251 en_US
dc.rights Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. en_US
dc.source Prof. Griffin via Erja Kajosalo en_US
dc.title Heteronuclear proton assisted recoupling en_US
dc.type Article en_US
dc.identifier.citation Paëpe, Gaël De et al. “Heteronuclear Proton Assisted Recoupling.” The Journal of Chemical Physics 134.9 (2011): 095101. © 2011 American Institute of Physics en_US
dc.contributor.department Massachusetts Institute of Technology. Department of Chemistry en_US
dc.contributor.department Francis Bitter National Magnet Laboratory en_US
dc.contributor.approver Griffin, Robert G.
dc.contributor.mitauthor Paepe, Gael De
dc.contributor.mitauthor Lewandowski, Jozef R.
dc.contributor.mitauthor Eddy, Matthew Thomas
dc.contributor.mitauthor Griffin, Robert Guy
dc.relation.journal Journal of Chemical Physics en_US
dc.identifier.mitlicense PUBLISHER_POLICY en_US
dc.eprint.version Final published version en_US
dc.type.uri http://purl.org/eprint/type/JournalArticle en_US
eprint.status http://purl.org/eprint/status/PeerReviewed en_US
dspace.orderedauthors Paëpe, Gaël De; Lewandowski, Józef R.; Loquet, Antoine; Eddy, Matt; Megy, Simon; Böckmann, Anja; Griffin, Robert G. en


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