Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution.
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Summary
The TROSY principle should benefit a variety of multidimensional solution NMR experiments, especially with future use of yet somewhat higher polarizing magnetic fields than are presently available, and thus largely eliminate one of the key factors that limit work with larger molecules.
- Type
- article
- Published
- 1997-11-11
- Cited by
- 2,172
- References
- 31
- Access
- Open access
- OpenAlex
- https://openalex.org/W2147281292
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:12130640
Keywords
Relaxation (psychology), Chemistry, Residual dipolar coupling, Anisotropy, Nuclear magnetic resonance
References
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- Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei
- The absence of "heme-heme" interactions in hemoglobin.
- Nuclear magnetic resonance solution structure of the fushi tarazu homeodomain from Drosophila and comparison with the Antennapedia homeodomain.
- Principles of nuclear magnetic resonance in one and two dimensions
- Effect of Anisotropic Hyperfine Interactions on Paramagnetic Relaxation in Liquids
- Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence
- Prospects for NMR of large proteins
- Pulse sequences for removal of the effects of cross correlation between dipolar and chemical-shift anisotropy relaxation mechanisms on the measurement of heteronuclear T1 and T2 values in proteins
- Spin—spin coupling and the conformational states of peptide systems
- Suppression of the effects of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms in the measurement of spin-spin relaxation rates
- NMR - this other method for protein and nucleic acid structure determination.
- Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
- A theoretical evaluation of the significance of scalar relaxation in coupled spin-12 systems in macromolecules
Cited by
- Structural Model of the Fe-Hydrogenase/Cytochromec 553 Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations*
- Correlation of backbone amide and side-chain (13)C resonances in perdeuterated proteins.
- Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653.
- Measuring 1H-1H and 1H-13C RDCs in methyl groups: example of pulse sequences with numerically optimized coherence transfer schemes.
- Optimal experiments for maximizing coherence transfer between coupled spins.
- Identification of the N- and C-terminal substrate binding segments of ferredoxin-NADP+ reductase by NMR.
- Ferredoxin/ferredoxin–thioredoxin reductase complex: Complete NMR mapping of the interaction site on ferredoxin by gallium substitution
- NMR methods for studying protein-protein interactions involved in translation initiation.
- Conformational dynamics of the KcsA potassium channel governs gating properties
- The role of protein 3D-structures in the drug discovery process.
- Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
- The Therapeutically Anti-prion Active Antibody-fragment scFv-W226: Paramagnetic Relaxation-Enhanced NMR Spectroscopy aided Structure Elucidation of the Paratope-epitope Interface
- Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain.
- Isotope labeling methods for large systems.
- Quadrupole central transition 17O NMR spectroscopy of biological macromolecules in aqueous solution.
- Intra- and intermolecular translocation of the bi-domain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR
- NMR spectroscopy to study the dynamics and interactions of CFTR.
- Multiple resonance heteronuclear decoupling under MAS: dramatic increase of spectral resolution at moderate magnetic field and MAS frequencies.
- An NMR method to study protein-protein interactions.
- The Interaction between tRNALys 3 and the Primer Activation Signal Deciphered by NMR Spectroscopy
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