Coupling Amplification in 2D MAS NMR and Its Application to Torsion Angle Determination in Peptides

Hong, Mei; Gross, John D.; Rienstra, Chad M.; Griffin, Robert G.; Kumashiro, Kristin K.; Schmidt‐Rohr, Klaus

doi:10.1006/jmre.1997.1242

Cited by 139 publications

(124 citation statements)

References 26 publications

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“…angles were measured under 6.5-kHz MAS by using the HNCH technique, with doubling of the NOH dipolar coupling to enhance the angular resolution (22,46). 1 HO 1 H homonuclear coupling was removed by an FSLG sequence (47).…”

Section: Ssnmr Spectroscopymentioning

confidence: 99%

“…The wrong angle is readily identified by the fact that it falls into either unpopulated regions of the Ramachandran diagram or the ␤-sheet region, which contradicts NMR chemical shifts. 15 NO 1 H dipolar couplings for orientation determination were obtained from a dipolar-doubled DIPSHIFT experiment (46,49,50) under 7-kHz MAS. An FSLG sequence with an effective field of 76.5 kHz was used for 1 H homonuclear decoupling.…”

Section: Ssnmr Spectroscopymentioning

confidence: 99%

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Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel

Cady

Hong

2008

Proc. Natl. Acad. Sci. U.S.A.

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110

141

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The M2 protein of influenza A virus forms a transmembrane proton channel important for viral infection and replication. Amantadine blocks this channel, thus inhibiting viral replication. Elucidating the high-resolution structure of the M2 protein and its change upon amantadine binding is crucial for designing antiviral drugs to combat the growing resistance of influenza A viruses against amantadine. We used magic-angle-spinning solid-state NMR to determine the conformation and dynamics of the transmembrane domain of the protein M2TMP in the apo-and amantadine-bound states in lipid bilayers. 13 C chemical shifts and torsion angles of the protein in 1,2-dilauroyl-sn-glycero-3-phosphatidylcholine (DLPC) bilayers indicate that M2TMP is ␣-helical in both states, but the average conformation differs subtly, especially at the G34 -I35 linkage and V27 side chain. In the liquid-crystalline membrane, the complexed M2TMP shows dramatically narrower lines than the apo peptide. Analysis of the homogeneous and inhomogeneous line widths indicates that the apo-M2TMP undergoes significant microsecond-time scale motion, and amantadine binding alters the motional rates, causing line-narrowing. Amantadine also reduces the conformational heterogeneity of specific residues, including the G34/I35 pair and several side chains. Finally, amantadine causes the helical segment N-terminal to G34 to increase its tilt angle by 3°, and the G34 -I35 torsion angles cause a kink of 5°in the amantadine-bound helix. These data indicate that amantadine affects the M2 proton channel mainly by changing the distribution and exchange rates among multiple low-energy conformations and only subtly alters the average conformation and orientation. Amantadine-resistant mutations thus may arise from bindingincompetent changes in the conformational equilibrium.high-resolution structure ͉ membrane protein ͉ solid-state NMR ͉ conformational heterogeneity ͉ chemical-shift perturbation

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Section: Ssnmr Spectroscopymentioning

confidence: 99%

Section: Ssnmr Spectroscopymentioning

confidence: 99%

Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel

Cady

Hong

2008

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

110

141

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“…The pulse program is simulated using SIPMSON, which indicates that the fitting remarktably depends on the 13 C CSA value and is insensitive to Euler angles or asymmetry parameters. The motional averaged 13 C-1 H dipolar couplings were measured using the Dipolar-chemical-shift (DIPSHIFT) experiment under 6 kHz MAS [35]. The pulse block of PMLG [56] was used to achieve 1 H homonuclear dipolar decoupling during the rotor period.…”

Section: Solid State Nmr Experimentsmentioning

confidence: 99%

“…Specifically, an array of techniques, including DIPSHIFT [35,36], 2D WISE [37], SUPER [38], 2 H-NMR [39], REDOR [40,41] and relaxation parameters measurements [42], have been well established to investigate the rigidity or mobility of a variety of functional (bio-)polymers. In recent years, lots of efforts have been made towards better understanding the structure-property relationship of different kinds of polymeric species at the atomic or molecular level using SSNMR.…”

Section: Introductionmentioning

confidence: 99%

Molecular Dynamics of Neutral Polymer Bonding Agent (NPBA) as Revealed by Solid-State NMR Spectroscopy

Hu¹,

Zhou

et al. 2014

Molecules

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Neutral polymer bonding agent (NPBA) is one of the most promising polymeric materials, widely used in nitrate ester plasticized polyether (NEPE) propellant as bonding agent. The structure and dynamics of NPBA under different conditions of temperatures and sample processing are comprehensively investigated by solid state NMR (SSNMR). The results indicate that both the main chain and side chain of NPBA are quite rigid below its glass transition temperature (T g ). In contrast, above the T g , the main chain remains relatively immobilized, while the side chains become highly flexible, which presumably weakens the interaction between bonding agent and the binder or oxidant fillers and in turn destabilizes the high modulus layer formed around the oxidant fillers. In addition, no obvious variation is found for the microstructure of NPBA upon aging treatment or soaking with acetone. These experimental results provide useful insights for understanding the structural properties of NPBA and its interaction with other constituents of solid composite propellants under different processing and working conditions.

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“…A metodologia usa a interação dipolar heteronuclear entre spins abundantes e spins raros ( 13 C-1 H, por exemplo) para obter tais informações (22).…”

Section: Dipshift -Dipolar Chemical Shift Correlationunclassified

Dinâmica molecular e formação de domínios em copolímeros em bloco estudados por RMN de alta e baixa resolução

Bezerra¹

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Coupling Amplification in 2D MAS NMR and Its Application to Torsion Angle Determination in Peptides

Cited by 139 publications

References 26 publications

Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel

Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel

Molecular Dynamics of Neutral Polymer Bonding Agent (NPBA) as Revealed by Solid-State NMR Spectroscopy

Dinâmica molecular e formação de domínios em copolímeros em bloco estudados por RMN de alta e baixa resolução

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