Selective Homonuclear Polarization Transfer in the Tilted Rotating Frame under Magic Angle Spinning in Solids

Takegoshi, K.; Nomura, Kaoru; Terao, Takehiko

doi:10.1006/jmre.1997.1191

Cited by 53 publications

(52 citation statements)

References 22 publications

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“…Broad-band homonuclear polarization transfer used the DREAM scheme (Verel et al, 1998), (Verel et al, 2001). Narrow-band homonuclear polarization transfer employed the rotational-resonance tickling (R 2 T) method (Takegoshi et al, 1995), (Takegoshi et al, 1997), (Costa et al, 1997), (Detken et al, 2001). Sign-discrimination in the indirect dimensions was accomplished using TPPI (Marion and Wuthrich, 1983).…”

Section: Nmr-spectroscopymentioning

confidence: 99%

“…For the identification of the 13 C resonances within a residue, broadband recoupling methods are usually applied (Bennett et al, 1992), , (Carravetta et al, 2000), (Verel et al, 1998), (Verel et al, 2001), . For the sequential assignment of the amino-acid residues, two-and three-dimensional correlation experiments are applied which make use of heteronuclear transfer by cross-polarization (CP) and homonuclear transfer by broad-band (vide supra) and narrowband dipolar recoupling schemes such as rotationalresonance tickling (R 2 T) (Takegoshi et al, 1995), (Takegoshi et al, 1997), (Costa et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

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13C, 15N Resonance Assignment of Parts of the HET-s Prion Protein in its Amyloid Form

Siemer¹,

et al. 2006

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The partial 15 N and 13 C solid-state NMR resonance assignment of the HET-s prion protein fragment 218-289 in its amyloid form is presented. It is based on experiments measured at MAS frequencies in the range of 20-40 kHz using exclusively adiabatic polarization-transfer schemes. The resonance assignment within each residue is based on two-dimensional 13 CA 13 C correlation spectra utilizing the DREAM mixing scheme. The sequential linking of the assigned residues used a set of two-and three-dimensional 15 NA 13 C correlation experiments. Almost all cross peaks visible in the spectra are assigned, but only resonances from 43 of the 78 amino-acid residues could be detected. The missing residues are thought to be highly disordered and/or highly dynamic giving rise to broad resonance lines that escaped detection in the experiments applied. The line widths of the observed resonances are narrow and comparable to line widths observed in micro-crystalline samples. The 43 assigned residues are located in two fragments of about 20 residues.Abbreviations: 2D -two-dimensional; 3D -three-dimensional; APHH -adiabatic-passage Hartmann-Hahn; CP -cross polarization; CW -continuous wave; DREAM -dipolar recoupling enhanced by amplitude modulation; HORROR -homonuclear rotary resonance; MAS -magic angle spinning; NMR -nuclear magnetic resonance; NOE -nuclear overhauser effect; PDSD -proton-driven spin diffusion; R 2 Trotational resonance tickling; RFDR -radio-frequency driven spin diffusion; TPPI -time-proportional phase increment; TRIS -tris(hydroxymethyl)aminomethane; XiX -X inverse X.

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Section: Nmr-spectroscopymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

13C, 15N Resonance Assignment of Parts of the HET-s Prion Protein in its Amyloid Form

Siemer¹,

et al. 2006

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“…24,25 A second approach is to use techniques that recouple only pairs of nuclei that have certain chemical shifts, thus converting a many-spin system to a two-spin system. Such frequency-selective recoupling techniques use weak rf irradiation, 26 simultaneous recoupling of dipole-dipole couplings and chemical shifts, [27][28][29] or alternating periods of dipolar (or scalar) recoupling and free precession under chemical shifts [30][31][32] to introduce dependences on NMR frequencies. Distances between non-bonded pairs of 13 C- 13 C nuclei in uniformly 13 C-labeled compounds have been measured accurately with frequency-selective recoupling techniques.…”

Section: Introductionmentioning

confidence: 99%

Zero-quantum stochastic dipolar recoupling in solid state nuclear magnetic resonance

Wang

Tycko

2012

The Journal of Chemical Physics

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We present the theoretical description and experimental demonstration of a zero-quantum stochastic dipolar recoupling (ZQ-SDR) technique for solid state nuclear magnetic resonance (NMR) studies of 13 C-labeled molecules, including proteins, under magic-angle spinning (MAS). The ZQ-SDR technique combines zero-quantum recoupling pulse sequence blocks with randomly varying chemical shift precession periods to create randomly amplitude-and phase-modulated effective homonuclear magnetic dipole-dipole couplings. To a good approximation, couplings between different 13 C spin pairs become uncorrelated under ZQ-SDR, leading to spin dynamics (averaged over many repetitions of the ZQ-SDR sequence) that are fully described by an orientation-dependent N × N polarization transfer rate matrix for an N-spin system, with rates that are inversely proportional to the sixth power of internuclear distances. Suppression of polarization transfers due to non-commutivity of pairwise couplings (i.e., dipolar truncation) does not occur under ZQ-SDR, as we show both analytically and numerically. Experimental demonstrations are reported for uniformly 13 C-labeled L-valine powder (at 14

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“…A panoply of resonance assignment experiments has been developed in liquid state NMR (1) and recent advances in homonuclear (2) and heteronuclear (3) dipolar recoupling schemes have yielded similar results in high resolution solid state NMR (ssNMR). Partial or complete resonance assignments have been reported for four proteins in the solid state: human ubiquitin (4,5), Bovine Pancreatic Trypsin Inhibitor (BPTI) (6), the SH3 domain of human α-spectrin (7), and the Light Harvesting Complex LHII from Rhodopseudomonas acidophilia-10050 (8).…”

mentioning

confidence: 96%

“…If κ = 0 (i.e., the evolution time period t 2 is not incremented) a single peak appears in ω 1 at Ω 1 as in the conventional HETCOR experiment. However, if κ > 0, the single resonance in ω 1 is split into two peaks, centered on Ω 1 and located at the sum and difference of the chemical shift offset of the two spins (Ω 1 + κΩ 2 and Ω 1 − κΩ 2 ) (vide infra). To avoid a corresponding decrease in resolution it is necessary to choose κ and the rf-carrier position such that the upfield (Ω 1 − κΩ 2 ) and downfield (Ω 1 + κΩ 2 ) components of the doublet are shifted to distinct regions of the spectrum.…”

mentioning

confidence: 99%

Triple Resonance Solid State NMR Experiments with Reduced Dimensionality Evolution Periods

Astrof

Lyon

Griffin

2001

Journal of Magnetic Resonance

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Selective Homonuclear Polarization Transfer in the Tilted Rotating Frame under Magic Angle Spinning in Solids

Cited by 53 publications

References 22 publications

13C, 15N Resonance Assignment of Parts of the HET-s Prion Protein in its Amyloid Form

13C, 15N Resonance Assignment of Parts of the HET-s Prion Protein in its Amyloid Form

Zero-quantum stochastic dipolar recoupling in solid state nuclear magnetic resonance

Triple Resonance Solid State NMR Experiments with Reduced Dimensionality Evolution Periods

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