An efficient 3D NMR technique for correlating the proton and15N backbone amide resonances with the α-carbon of the preceding residue in uniformly15N/13C enriched proteins

  title={An efficient 3D NMR technique for correlating the proton and15N backbone amide resonances with the $\alpha$-carbon of the preceding residue in uniformly15N/13C enriched proteins},
  author={Adriaan Bax and Mitsuhiko Ikura},
  journal={Journal of Biomolecular NMR},
  • A. BaxM. Ikura
  • Published 1 May 1991
  • Biology
  • Journal of Biomolecular NMR
SummaryA 3D NMR technique is described which correlates the amide proton and nitrogen resonances of an amino acid residue with the Cα chemical shift of its preceding residue. The technique uses a relay mechanism, transferring magnetization from15N to13Cα via the intervening carbonyl nucleus. This method for obtaining sequential connectivity is less sensitive to large line widths than the alternative HNCA experiment. The technique is demonstrated for the protein calmodulin, complexed with a 26… 

3D Triple-resonance NMR techniques for the sequential assignment of NH and 15N resonances in 15N- and 13C-labelled proteins

SummaryTwo new 3D 1H-15N-13C triple-resonance experiments are presented which provide sequential cross peaks between the amide proton of one residue and the amide nitrogen of the preceding and

Backbone assignment of perdeuterated proteins using long-range H/C-dipolar transfers

  • R. Linser
  • Chemistry
    Journal of biomolecular NMR
  • 2012
This work proposes an approach towards sequential assignment of perdeuterated proteins based on long-range 1H/13C Cross Polarization transfers that gives rise to H/N-separated correlations involving Cα, Cβ, and CO chemical shifts of both, intra- and interresidual contacts, and thus connecting adjacent residues independent of transverse relaxation times.

A 4D HCCH-TOCSY experiment for assigning the side chain1H and13C resonances of proteins

A 4D HCCH-TOCSY experiment is described for correlating and assigning the1H and13C resonances of protein amino acid side chains that has several advantages over 3D versions of the experiment, including automation of resonance assignments.

Sequential assignment of the backbone nuclei (1H,15N and13C) of c-H-ras p21 (1–166).GDP using a novel 4D NMR strategy

This work reports here the sequential assignment of the backbone nuclei in a truncated form of the 21-kD gene product, using the recently proposed 4D NMR strategy (Boucher et al., 1992).

Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.

A general strategy for assigning backbone and side-chain resonances in a perdeuterated large protein is outlined, whereby this information can be used to glean more detailed structural information from the partially or fully protonated protein equivalent.

31P–1H correlation and resonance assignments along the DNA backbone: three‐dimensional implementation of heteronuclear long‐range correlation experiment

A three‐dimensional heteronuclear NMR technique to correlate 31P spins with 1H along the backbone of DNA is described. The approach is based on a 31P–1H heteronuclear long‐range correlation (HELCO)

Bidirectional band-selective magnetization transfer along the protein backbone doubles the information content of solid-state NMR correlation experiments

Significant reductions in acquisition times are realised, allowing the acquisition of a single 3D-NCOCA spectrum suitable for a full backbone resonance assignment of GB3 in less than 24 h.



A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

It is demonstrated that the combined use of four new types of heteronuclear 3D NMR spectra together with the previously described HOHAHA-HMQC 3D experiment can provide unambiguous sequential assignment of protein backbone resonances.

Concerted two-dimensional NMR approaches to hydrogen-1, carbon-13, and nitrogen-15 resonance assignments in proteins.

Carbon-carbon and proton-carbon couplings can be used to bridge the aromatic and aliphatic parts of proton spin systems; this avoids possible ambiguities that may result from the use of nuclear Overhauser effects to assign aromatic amino acid signals.

Protein carbon-13 spin systems by a single two-dimensional nuclear magnetic resonance experiment.

Spin systems of 75 of the 98 amino acid residues in a protein, oxidized Anabaena 7120 ferredoxin (molecular weight 11,000), were identified by this approach, which represents a key step in an improved methodology for assigning protein nuclear magnetic resonance spectra.

Principles of nuclear magnetic resonance in one and two dimensions

List of notation Introduction The dynamics of nuclear spin systems Manipulation of nuclear spin Hamiltonians One-dimensional Fourier spectroscopy Multiple-quantum transitions Two-dimensional Fourier