|
authors |
Agarwal, V; Sardo, M; Scholz, I; Bockmann, A; Ernst, M; Meier, BH |
|
nationality |
International |
|
journal |
JOURNAL OF BIOMOLECULAR NMR |
|
author keywords |
Solid-state NMR; Heteronuclear correlation; PAIN-CP; RESORT; Heteronuclear RESORT |
|
keywords |
SOLID-STATE NMR; ANGLE-SPINNING NMR; NUCLEAR-MAGNETIC-RESONANCE; PROTEIN-STRUCTURE DETERMINATION; ESCHERICHIA-COLI THIOREDOXIN; 3D STRUCTURE DETERMINATION; ROTATING SOLIDS; CROSS-POLARIZATION; AMYLOID FIBRILS; CORRELATION SPECTROSCOPY |
|
abstract |
In this article, we describe third-spin assisted heteronuclear recoupling experiments, which play an increasingly important role in measuring long-range heteronuclear couplings, in particular N-15-C-13, in proteins. In the proton-assisted insensitive nuclei cross polarization (PAIN-CP) experiment (de PaA << pe et al. in J Chem Phys 134:095101, 2011), heteronuclear polarization transfer is always accompanied by homonuclear transfer of the proton-assisted recoupling (PAR) type. We present a phase-alternating experiment that promotes heteronuclear (e.g. N-15 -> C-13) polarization transfer while simultaneously minimizing homonuclear (e.g.C-13 -> C-13) transfer (PAIN without PAR). This minimization of homonuclear polarization transfer is based on the principle of the resonant second-order transfer (RESORT) recoupling scheme where the passive proton spins are irradiated by a phase-alternating sequence and the modulation frequency is matched to an integer multiple of the spinning frequency. The similarities and differences between the PAIN-CP and this het-RESORT experiment are discussed here. |
|
publisher |
SPRINGER |
|
issn |
0925-2738 |
|
year published |
2013 |
|
volume |
56 |
|
issue |
4 |
|
beginning page |
365 |
|
ending page |
377 |
|
digital object identifier (doi) |
10.1007/s10858-013-9756-4 |
|
web of science category |
Biochemistry & Molecular Biology; Spectroscopy |
|
subject category |
Biochemistry & Molecular Biology; Spectroscopy |
|
unique article identifier |
WOS:000323661800008
|
