A Method for Dihedral Angle Measurement in Solids: Rotational Resonance NMR of a Transition-State Inhibitor of Triose Phosphate Isomerase

Tomita, York; O'Connor, Edward J.; McDermott, Ann E.

doi:10.1021/ja00098a039

Cited by 45 publications

(83 citation statements)

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“…Figure 6 defines the reference frames which are used to define the rotation of the 13 C chemical shift tensor samples with a powder-type distribution is limited to relative orientations of tensors with respect to each other, for exam-(CST) of methylene into the rotor-fixed coordinate system. The principal axis system of the CST coincides with the ple, in the form of torsional and dihedral angles (66)(67)(68).…”

Section: Figmentioning

confidence: 98%

Magic Angle-Oriented Sample Spinning (MAOSS): A New Approach toward Biomembrane Studies

Glaubitz¹,

Watts²

1998

Journal of Magnetic Resonance

120

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Section: Figmentioning

confidence: 98%

Magic Angle-Oriented Sample Spinning (MAOSS): A New Approach toward Biomembrane Studies

Glaubitz¹,

Watts²

1998

Journal of Magnetic Resonance

120

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“…Heteronuclear dipolar interactions are evaluate relative directions of chemical bonds and functional decoupled by an RF field for 1 H. Homonuclear dipolar cougroups in crystals and polymers (3)(4)(5)(6)(7)(8). If such an orientation plings for 13 C are averaged by MAS during the constantfor carbons connected by a covalent bond is determined, time period independently of t 1 (13), if the effects combined information on the dihedral angle can be obtained (9). How-with chemical shifts are disregarded.…”

Section: Recovery Of Chemical-shift Anisotropy Under Mas Sotropic Intmentioning

confidence: 99%

Multidimensional Solid-State Nuclear Magnetic Resonance for Correlating Anisotropic Interactions under Magic-Angle Spinning Conditions

Fujiwara

Shimomura

Akutsu

1997

Journal of Magnetic Resonance

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“…For rotational-resonance magnetization-exchange experiments, total experiment times were kept constant by introducing a variable delay while I3C magnetization was stored along the z-axis before inversion (Tomita et al, 1994). This lead to the same average power dissipation due to proton decoupling in all experiments, thus eliminating radio-frequency heating effects as a possible source of error in the measurements.…”

Section: Data Acquisitionmentioning

confidence: 99%

Solid‐state NMR studies of the prion protein H1 fragment

et al. 1996

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Conformational changes in the prion protein (PrP) seem to be responsible for prion diseases. We have used conformation-dependent chemical-shift measurements and rotational-resonance distance measurements to analyze the conformation of solid-state peptides lacking long-range order, corresponding to a region of PrP designated H I . This region is predicted to undergo a transformation of secondary structure in generating the infectious form of the protein. Solid-state NMR spectra of specifically '3C-enriched samples of HI, residues 109-122 (MKHMAGAAAAGAVV) of Syrian hamster PrP, have been acquired under cross-polarization and magic-angle spinning conditions. Samples lyophilized from 50% acetonitrile/50% water show chemical shifts characteristic of a 0-sheet conformation in the region corresponding to residues 112-121, whereas samples lyophilized from hexafluoroisopropanol display shifts indicative of a-helical secondary structure in the region corresponding to residues 113-1 17. Complete conversion to the helical conformation was not observed and conversion from a-helix back to 0-sheet, as inferred from the solid-state NMR spectra, occurred when samples were exposed to water. Rotational-resonance experiments were performed on seven doubly I3C-labeled H1 samples dried from water. Measured distances suggest that the peptide is in an extended, possibly &strand, conformation. These results are consistent with the experimental observation that P r P can exist in different conformational states and with structural predictions based on biological data and theoretical modeling that suggest that HI may play a key role in the conformational transition involved in the development of prion diseases.

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A Method for Dihedral Angle Measurement in Solids: Rotational Resonance NMR of a Transition-State Inhibitor of Triose Phosphate Isomerase

Cited by 45 publications

References 0 publications

Magic Angle-Oriented Sample Spinning (MAOSS): A New Approach toward Biomembrane Studies

Magic Angle-Oriented Sample Spinning (MAOSS): A New Approach toward Biomembrane Studies

Multidimensional Solid-State Nuclear Magnetic Resonance for Correlating Anisotropic Interactions under Magic-Angle Spinning Conditions

Solid‐state NMR studies of the prion protein H1 fragment

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