Accuracy Limitations on Internuclear Distances Measured by REDOR

Naito, Akira; Saitô, Hazime

doi:10.1002/9780470034590.emrstm0002

Cited by 2 publications

(2 citation statements)

References 35 publications

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“…15 N rotational-echo double-resonance (REDOR) spectra were measured using an xy-4 irradiation pulse to compensate for the errors of the flip-angle, off-resonance effect, and fluctuation of the radio-frequency field for 13 C nuclei (24). The lengths of p pulses for 13 C and 15 N nuclei were 12.3 and 13.5 ms, respectively, and the recycle time was 4 s. The proton decoupling amplitude was 65 kHz.…”

Section: Nmr Measurementsmentioning

confidence: 99%

Dynamic Structure of Bombolitin II Bound to Lipid Bilayers as Revealed by Solid-state NMR and Molecular-Dynamics Simulation

Toraya

Javkhlantugs

Mishima

et al. 2010

Biophysical Journal

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Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) membranes were determined by solid-state (31)P and (13)C NMR spectroscopy. (31)P NMR spectra showed that BLT2-DPPC membranes were disrupted into small particles below the gel-to-liquid crystalline phase transition temperature (T(c)) and fused to form a magnetically oriented vesicle system where the membrane surface is parallel to the magnetic fields above the T(c). (13)C NMR spectra of site-specifically (13)C-labeled BLT2 at the carbonyl carbons were observed and the chemical shift anisotropies were analyzed to determine the dynamic structure of BLT2 bound to the magnetically oriented vesicle system. It was revealed that the membrane-bound BLT2 adopted an α-helical structure, rotating around the membrane normal with the tilt angle of the helical axis at 33°. Interatomic distances obtained from rotational-echo double-resonance experiments further showed that BLT2 adopted a straight α-helical structure. Molecular dynamics simulation performed in the BLT2-DPPC membrane system showed that the BLT2 formed a straight α-helix and that the C-terminus was inserted into the membrane. The α-helical axis is tilted 30° to the membrane normal, which is almost the same as the value obtained from solid-state NMR. These results suggest that the membrane disruption induced by BLT2 is attributed to insertion of BLT2 into the lipid bilayers.

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Section: Nmr Measurementsmentioning

confidence: 99%

Dynamic Structure of Bombolitin II Bound to Lipid Bilayers as Revealed by Solid-state NMR and Molecular-Dynamics Simulation

Toraya

Javkhlantugs

Mishima

et al. 2010

Biophysical Journal

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“…(1). As a result, the rotational-echo double-resonance (REDOR) method [88,89] was used to measure the interatomic distance between [1-13 C]Val8 and [ 15 N]Leu13 to further identify the bending α-helical structure of melittin resulting in interhelical angles of 126°and 119°in DLPC and DPPC membranes, respectively. These analyses led to the conclusion that the α-helices of melittin molecules penetrate the hydrophobic core of the bilayers incompletely as a pseudo-transmembrane structure, inducing fusion and disruption of the vesicles.…”

Section: Melittinmentioning

confidence: 99%