ArticleThe Journal of chemical physics2011
Heteronuclear proton assisted recoupling.
Article in The Journal of chemical physics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 59 citations in OpenAlex.
- Atomic Structure of GNNQQNY Nanocrystals: A Validated Approach for Polymorphic Amyloids.The journal of physical chemistry letters · 2025Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Homonuclear J-couplings and heteronuclear structural constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Unveiling Charge-Pair Salt-Bridge Interaction Between GAGs and Collagen Protein in Cartilage: Atomic Evidence from DNP-Enhanced ssNMR at Natural Isotopic Abundance.Journal of the American Chemical Society · 2024Article
- Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy: Advances in Methodology and Applications.Chemical reviews · 2023Review
- Solid-State NMR Structure of Amyloid-β Fibrils.Methods in molecular biology (Clifton, N.J.) · 2023Article
- From Angstroms to Nanometers: Measuring Interatomic Distances by Solid-State NMR.Chemical reviews · 2022Review
- Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability.The Journal of biological chemistry · 2020Article
- Pulsed Third-Spin-Assisted Recoupling NMR for Obtaining Long-RangeThe journal of physical chemistry. B · 2020Article
- EfficientThe journal of physical chemistry. B · 2018Article
- Article
- Proton-Assisted Recoupling (PAR) in Peptides and Proteins.The journal of physical chemistry. B · 2017Article
- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
- Atomic-resolution three-dimensional structure of amyloid β fibrils bearing the Osaka mutation.Angewandte Chemie (International ed. in English) · 2015Article
- Demonstration of a common indole-based aromatic core in natural and synthetic eumelanins by solid-state NMR.Organic & biomolecular chemistry · 2014Article
- Mechanism of dilute-spin-exchange in solid-state NMR.The Journal of chemical physics · 2014Article
- Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity.PloS one · 2014Article
- Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.Journal of the American Chemical Society · 2013Article
- PAIN with and without PAR: variants for third-spin assisted heteronuclear polarization transfer.Journal of biomolecular NMR · 2013Article
- Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra.The Journal of chemical physics · 2013Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
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=2×10.4 kDa). The spectra acquired at high magic angle spinning frequencies (ω(r)∕2π>20 kHz) and magnetic fields (ω(0H)∕2π=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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.