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At least 523 records · Page 29Linked to original sources
PubMed2006

Microcoil high-resolution magic angle spinning NMR spectroscopy.

We report the construction of a dual-channel microcoil nuclear magnetic resonance probehead allowing magic-angle spinning for mass-limited samples. With coils down to 235 mum inner diameter, this allows high-resolution solid-state NMR spectra to be obtained for amounts of materials of a few nanoliters. This is demonstrated by the carbon-13 spectrum of a tripeptide and a single silk rod, prepared from the silk gland of the Bombyx mori silkworm. Furthermore, the microcoil allows for radio frequency field strengths well beyond current probe technology, aiding in getting the highest possible resolution by efficiently decoupling the observed nuclei from the abundantly present proton nuclei.

Alanine↗
PubMed2006

Proton-selective 17O-1H distance measurements in fast magic-angle-spinning solid-state NMR spectroscopy for the determination of hydrogen bond lengths.

We present a proton-selective method to determine 17O-1H distances in organic, biological, and biomimetic materials by fast magic-angle-spinning solid-state NMR spectroscopy. This method allows the determination of internuclear distances between specific (17O, 1H) spin pairs selectively. It enables the estimation of medium-range 17O...1H distances across hydrogen bonds in the presence of short-range 17O-1H contacts sharing the same 17O site. The method employs the newly developed symmetry-based radiofrequency pulse sequence SR%@mt;sys@%4%@sx@%1%@be@%2%@sxx@%%@mx@% applied to the protons to achieve heteronuclear dipolar recoupling, while simultaneously decoupling the homonuclear proton dipolar interactions. Fast MAS (50 kHz) and high static magnetic fields (18.8 T) achieve the required proton spectral resolution.

Hydrogen Bonding↗
PubMed2003

Post-mortem changes in porcine M. longissimus studied by solid-state 13C cross-polarization magic-angle spinning nuclear magnetic resonance spectroscopy.

Solid-state (13)C cross-polarization (CP) magic-angle spinning (MAS) nuclear magnetic resonance (NMR) experiments are carried out for the first time on rapidly frozen muscle biopsies taken in M. longissimus in vivo and at 1 min, 45 min, and 24 h post-mortem from three pigs. Two of the pigs were CO(2)-stunned (control animals), and one was pre-slaughter-stressed (treadmill exercise) followed by electrical stunning to induce difference in metabolism post-mortem. (13)C resonance signals from saturated and unsaturated carbons in fatty acids, carboxylic carbons, and carbons in lactate and glycogen are identified in the solid-state NMR spectra. The (13)C CP MAS spectra obtained for post-mortem samples of the stressed, electrically stunned pig differ significantly from the post-mortem control samples, as the intensity of a resonance line appearing at 30 ppm, assigned to carbons of the methylene chains, is reduced for the stressed pig. This spectral difference is probably due to changes in lipid mobility and indicates altered membrane properties in the muscle of the stressed/electrically stunned animal when compared with the control animals already 1 min post-mortem. In addition, the post-mortem period changes in glycogen carbons can be estimated from the (13)C CP MAS spectra, yielding a correlation of r = 0.74 to subsequent biochemical determination of the glycogen content.

Animals↗
PubMed2004

Dynamic high-resolution 1H and 31P NMR spectroscopy and 1H T2 measurements in postmortem rabbit muscles using slow magic angle spinning.

Postmortem changes in rabbit muscle tissue with different glycogen status (normal vs low) were followed continuously from 13 min postmortem until 8 h postmortem and again 20 h postmortem using simultaneous magic angle spinning (1)H and (31)P NMR spectroscopy together with measurement of the transverse relaxation time, T(2), of the muscle water. The (1)H metabolite spectra were measured using the phase-altered spinning sidebands (PASS) technique at a spinning rate of 40 Hz. pH values calculated from the (31)P NMR spectra using the chemical shifts of the C-6 line of histidine in the (1)H spectra and the chemical shifts of inorganic phosphate in the (31)P spectra confirmed the different muscle glycogen status in the tissues. High-resolution (1)H spectra obtained from the PASS technique revealed the presence of a new resonance line at approximately 6.8 ppm during the postmortem period, which were absent in muscles with low muscle glycogen content. This new resonance line may originate from the aminoprotons in creatine, and its appearance may be a result of a pH effect on the exchange rate between the amino and the water protons and thereby the NMR visibility. Alternatively, the new resonance line may originate from the aromatic protons in tyrosine, and its appearance may be a result of a pH-induced protein unfolding exposing hydrophobic amino acid residues to the aqueous environment. Further studies are needed to evaluate these hypotheses. Finally, distributed analysis of the water T(2) relaxation data revealed three relaxation populations and an increase in the population believed to reflect extramyofibrillar water through the postmortem period. This increase was significantly reduced (p < 0.0001) in samples from animals with low muscle glycogen content, indicating that the pH is controlling the extent of postmortem expulsion of water from myofibrillar structures. The significance of the postmortem increase in the amount extramyofibrillar water on the water-holding capacity was verified by centrifugation, which showed a reduced centrifugation loss in muscles with low preslaughter glycogen status (0.9 vs 1.9%, p = 0.07).

Animals↗
PubMed2005

Origin of the high-frequency resonances in 1H NMR spectra of muscle tissue: an in vitro slow magic-angle spinning study.

High-resolution slow magic-angle spinning (150 Hz) 1H PASS NMR spectroscopy is performed on intact excised rat m. tibialis anterior. Untreated muscles and muscles in vitro incubated in Krebs-Ringers buffer based on deuterium oxide are investigated. In the high-frequency region of the 1H NMR spectra, resonances from H4 (approximately 7.1-7.2 ppm) and H2 (approximately 8.2-8.5 ppm) in histidine are observed. In addition, a resonance appears at 6.7 ppm for the untreated muscles. However, this resonance is absent in muscles following incubation in deuterium oxide. On the basis of its behavior in deuterium oxide combined with supplementary measurements for creatine solutions, the 6.7 ppm resonance is ascribed to the amino protons in creatine. Moreover, the present study demonstrates that the observation of the 6.7 ppm resonance depends on pH, which explains earlier reports stating its occasional appearance. Finally, measurements on solutions of ATP/AMP and histidine indicate that both ATP/AMP and histidine contribute to the resonances at approximately 8.2-8.5 ppm in the 1H NMR spectra of muscle tissue.

Adenosine Triphosphate↗
PubMed2000

Antifeedant and mosquitocidal compounds from Delphinium x cultorum cv. Magic fountains flowers.

Six volatile compounds, ethylmethylbenzene (1), 1-isopentyl-2,4, 5-trimethylbenzene (2), 2-(hex-3-ene-2-one)phenylmethyl ketone (3), E and Z isomers of 3-butylidene-3H-isobenzofuran-1-one (4 and 5), and 2-penten-1-ylbenzoic acid (6), were isolated from the mosquitocidal hexane extract of Delphinium x cultorum cv. Magic Fountains flowers. In addition, the ethyl acetate extract, which displayed corn earworm antifeedant activity, yielded 4-hydroxybenzoic acid (7) and bis(4-hydroxyphenyl)methanol (8). However, compounds 7 and 8 were not biologically active.

Animals↗
PubMed2000

Quantitative monitoring of solid phase organic reactions by high-resolution magic angle spinning NMR spectroscopy

Three possible high-resolution magic angle spinning (HR MAS) NMR experiments to quantitatively monitor a solid phase supported Horner-Emmons reaction are presented. In the first experiment we follow the solid phase reaction in deuterated solvent directly in the NMR rotor. The second quantification is done by reconditioning of a few milligrams of resin from an undefined reaction vessel by washing, drying, and reswelling in deuterated solvent, and the evaluation of the amount of resin bound structures by comparing to an external standard. The third experiment represents the first analytical quantification of resin-bound structures without any sample preparation, except the transfer of resin-solvent suspension (large excess of reagents in protonated dimethylformamide) from the reaction vessel to the NMR rotor.

Journal Article↗
PubMed2005

Measurement of NMR cross-polarization (CP) rate constants in the slow CP regime: relevance to structure determinations of zeolite-sorbate and other complexes by cp magic-angle spinning NMR.

When analyzing I --> S variable contact time cross-polarization (CP) curves, the spin dynamics are usually assumed to be describable in the "fast CP regime" in which the growth of the S spin magnetization is governed by the rate of cross polarization while its decay is governed by the rate of I spin T1rho relaxation. However, in the investigation of the structures of zeolite-sorbate and other complexes by polarization transfer this will not necessarily be the case. We discuss the measurement of I --> S CP rate constants under the "slow CP regime" in which the rate of T1rho relaxation is fast compared to the rate of cross polarization, leading to a reversal of the usual assumptions such that the rate or growth is governed by the rate of I spin T1rho relaxation while the decay is governed by the rate of cross polarization (and the S spin T1rho relaxation). It is very important to recognize when a system is in the slow CP regime, as an analysis assuming the normal fast CP will lead to erroneous data. However, even when the slow CP regime is recognized, it is difficult to obtain absolute values for the CP rate constants from fits to standard CP curves, since the CP rate constant is correlated to the scaling factor, the contribution from 29Si T1rho relaxation is ignored, and it is difficult to obtain reliable data at very long contact times. The use of a 29Si{1H} CP "drain" or "depolarization" experiment, which measures absolute values of the CP rate constants, is therefore proposed as being most appropriate for theses situations. To illustrate the importance of these observations, measurements of the 1H-29Si CP rate constants in the p-dichlorobenzene/ZSM-5 sorbate-zeolite complex by 29Si{1H} CP and CP drain magic-angle spinning (MAS) NMR experiments are presented and compared and used to determine the location of the guest sorbate molecules in the cavities of the host zeolite framework.

Journal Article↗
PubMed2005

95Mo magic angle spinning NMR at high field: improved measurements and structural analysis of the quadrupole interaction in monomolybdates and isopolymolybdates.

In this study, 95Mo quadrupole couplings in various molydbates were measured easily and accurately with magic angle spinning (MAS) NMR under a directing field of 19.6 T. The resonance frequency of 54 MHz was sufficiently high to remove acoustic ringing artifacts, and the spectra could be analyzed in the usual terms of chemical shift and quadrupolar line shapes. For monomolybdates and molybdite, the quadrupole coupling dominated the NMR response, and the quadrupole parameters could be measured with better accuracy than in previous lower field studies. Moreover, despite the low symmetry of the molybdenum coordination, the usefulness of such measurements to probe molybdenum environments was established by ab initio density functional theory (DFT) calculations of the electric field gradient from known structures. The experimental NMR data correlated perfectly with the refined structures. In isopolymolybdates, the resonances were shapeless and DFT calculations were impossible because of the large and low symmetry unit cells. Nevertheless, empirical but clear NMR signatures were obtained from the spinning sidebands analysis or the MQMAS spectra. This was possible for the first time thanks to the improved baseline and sensitivity at high fields. With the generalization of NMR spectrometers operating above 17 T, it was predicted that 95Mo MAS NMR could evolve as a routine characterization tool for ill-defined structures such as supported molybdates in catalysis.

Journal Article↗
PubMed2005

Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.

De novo site-specific 13C and 15N backbone and sidechain resonance assignments are presented for uniformly enriched E. coli thioredoxin, established using two-dimensional homo- and heteronuclear solid-state magic angle spinning NMR correlation spectroscopy. Backbone dihedral angles and secondary structure were derived from the statistical analysis of the secondary chemical shifts, and are in good agreement with solution values for the intact full-length thioredoxin, with the exception of a small number of residues located at the termini of the individual secondary structure elements. A large number of cross-peaks observed in the DARR spectra with long mixing times correspond to the pairs of carbon atoms separated by 4-6 angstroms, suggesting that DARR could be efficiently employed for observation of medium- and long-range correlations. The 108 amino acid residue E. coli thioredoxin is the largest uniformly enriched protein assigned to this degree of completeness by solid-state NMR spectroscopy to date. It is anticipated that with a combination of two-dimensional correlation experiments and high magnetic fields, resonance assignments and secondary structure can be generally derived for other noncrystalline proteins.

Carbon Isotopes↗
PubMed2006

Multinuclear solid-state high-resolution and 13C -{27Al} double-resonance magic-angle spinning NMR studies on aluminum alkoxides.

A combination of 27Al magic-angle spinning (MAS)/multiple quantum (MQ)-MAS, 13C-1H CPMAS, and 13C-{27Al} transfer of population in double-resonance (TRAPDOR) nuclear magnetic resonance (NMR) were used for the structural elucidation of the aluminum alkoxides aluminum ethoxide, aluminum isopropoxide, and aluminum tertiarybutoxide. Aluminum alkoxides exist as oligomers with aluminum in different coordinations. High-resolution 27Al MAS NMR experiments with high-spinning speed distinguished the aluminum atoms in different environments. The 27Al MAS NMR spectrum gave well-resolved powder patterns with different coordinations. Z-filter MQ-MAS was performed to obtain the number and types of aluminum environments in the oligomeric structure. 13C-1H CPMAS chemical shifts resolved the different carbon species (-CH3, =CH2, =CH-, and =C=) in the structures. 13C-{27Al} TRAPDOR experiments were employed to obtain relative Al-C dipolar interactions and to distinguish between terminal and bridging alkoxides in the crystallographic structures. The complete characterization of selected aluminum alkoxides using advanced NMR methods has evidenced the tetrameric structure for aluminum isopropoxide and the dimeric structure for aluminum tertiary-butoxide, as reported in the literature, and proposed a polymeric structure for aluminum ethoxide.

Journal Article↗
PubMed2006

Determinations of 15N chemical shift anisotropy magnitudes in a uniformly 15N,13C-labeled microcrystalline protein by three-dimensional magic-angle spinning nuclear magnetic resonance spectroscopy.

Amide 15N chemical shift anisotropy (CSA) tensors provide quantitative insight into protein structure and dynamics. Experimental determinations of 15N CSA tensors in biologically relevant molecules have typically been performed by NMR relaxation studies in solution, goniometric analysis of single-crystal spectra, or slow magic-angle spinning (MAS) NMR experiments of microcrystalline samples. Here we present measurements of 15N CSA tensor magnitudes in a protein of known structure by three-dimensional MAS solid-state NMR. Isotropic 15N, 13C alpha, and 13C' chemical shifts in two dimensions resolve site-specific backbone amide recoupled CSA line shapes in the third dimension. Application of the experiments to the 56-residue beta1 immunoglobulin binding domain of protein G (GB1) enabled 91 independent determinations of 15N tensors at 51 of the 55 backbone amide sites, for which 15N-13C alpha and/or 15N-13C' cross-peaks were resolved in the two-dimensional experiment. For 37 15N signals, both intra- and interresidue correlations were resolved, enabling direct comparison of two experimental data sets to enhance measurement precision. Systematic variations between beta-sheet and alpha-helix residues are observed; the average value for the anisotropy parameter, delta (delta = delta(zz) - delta(iso)), for alpha-helical residues is 6 ppm greater than that for the beta-sheet residues. The results show a variation in delta of 15N amide backbone sites between -77 and -115 ppm, with an average value of -103.5 ppm. Some sites (e.g., G41) display smaller anisotropy due to backbone dynamics. In contrast, we observe an unusually large 15N tensor for K50, a residue that has an atypical, positive value for the backbone phi torsion angle. To our knowledge, this is the most complete experimental analysis of 15N CSA magnitude to date in a solid protein. The availability of previous high-resolution crystal and solution NMR structures, as well as detailed solid-state NMR studies, will enhance the value of these measurements as a benchmark for the development of ab initio calculations of amide 15N shielding tensor magnitudes.

Nitrogen Isotopes↗
PubMed2006

Probing local environments in paramagnetic europium-substituted Keggin solids by 31P magic angle spinning NMR spectroscopy.

Paramagnetic Eu-substituted Keggin oxopolytungstates crystallize in different forms, determined by the nature of the counterions. The crystal packing is in turn responsible for the variations in the geometry of paramagnetic Eu sites with respect to the anion core. We probed the paramagnetic environments in a series of Eu-substituted Keggin solids, by 31P magic angle spinning NMR spectroscopy. 31P spinning sideband envelopes are dominated by the electron-nuclear dipolar interaction. For the compounds under investigation, both the magnitude and the asymmetry parameter of the electron-nuclear dipolar coupling tensor are sensitive to the mutual arrangements of paramagnetic Eu sites in the crystal lattice. and also report on the stoichiometry of the anion. The electron-nuclear dipolar coupling tensors were calculated from the crystallographic coordinates and the experimentally determined effective magnetic moments, assuming a point dipole approximation. The computed tensors are in very good agreement with the experimental spectra. Furthermore, the P-Eu distance estimates, accurate to within 0.06-0.12 A, can be obtained directly from the magnitude of the electron-nuclear dipolar coupling. This work demonstrates that 31P MAS NMR spectroscopy is a useful probe for investigating local environments in paramagnetic Keggin solids.

Europium↗
PubMed2006

Low-frequency cooperative dynamics in L-, D-, and DL-alanine crystals: a 13C and 15N cross-polarization magic-angle-spinning NMR study.

Knowledge of the dynamical changes in molecular configurations in various amino acid structures over a wide range of time scales is important since such changes may influence the structural transformations and the diverse biological functionalities of proteins. Using the temperature dependence of the rotating-frame NMR spin-lattice relaxation times T(1rho) of protons as a probe, we have investigated the low-frequency (approximately 60-100 kHz) dynamics in the crystal structures of L-, D-, and DL- alanine (C(12)H(28)O(8)N(4)) polymorphs. The proton relaxation times T(1rho) were obtained from (13)C <-- (1)H and (15)N <-- (1)H cross-polarization magic-angle-spinning NMR experiments over a temperature range of 192-342 K. The data reveal that the time scales of these low-frequency dynamical processes are distinctly different from the localized, high-frequency rotational motion of methyl and amine groups. The strongly asymmetric T(1rho) versus temperature curves and the subtle dynamical differences between the DL-alanine and the L- and d-enantiomorphs indicate that these low-frequency processes are cooperative in nature and are sensitive to molecular packing.

Alanine↗
PubMed1997

A cross-polarization magic-angle spinning 13C NMR characterization of the stable solid-state forms of cimetidine.

Proton decoupled, cross-polarization magic-angle spinning 13C NMR spectra of four polymorphic forms (A, B, C, and D) and a monohydrate form (M1) of the histamine H2 antagonist cimetidine were obtained, and the chemical shifts of the various forms were tabulated. A modified polarization inversion pulse sequence was used to distinguish quaternary, methine, methylene, and methyl carbon resonances and thereby assist spectral assignment. It is also shown that the solid-state form of cimetidine in a commercial formulation can be reliably ascertained by NMR, despite the presence in the spectrum of signals from organic excipients that are much more intense than those from the compound.

Carbon Isotopes↗
PubMed1999

Sulfathiazole polymorphism studied by magic-angle spinning NMR.

The literature on sulfathiazole polymorphs has many confusions and inconsistencies. These are largely resolved by the distinctive appearance of (13)C magic-angle spinning NMR spectra, which immediately show the number of molecules in the crystallographic asymmetric unit. The spectra presented include those of a newly-recognized form. The assignments of the spectra are established and discussed in relation to such factors as electronic structure of the aromatic ring, second-order quadrupolar effects originating from the nitrogen nuclei, and hydrogen bonding. The results are compared to literature information on the crystal structures. When the amino group acts as a hydrogen bond acceptor, there is a shielding effect on C-4 to the extent of ca. 8 ppm (which should be compared to a further shielding by ca. 10 ppm for sulfathiazole sulfate). The fact that the spectrum of form III is similar to the sum of those of forms IV and V is rationalized in relation to the crystal structures. Some surprising variability of spectra with temperature and with specific sample is reported.

Carbon Isotopes↗
PubMed2005

Tethered or adsorbed supported lipid bilayers in nanotubes characterized by deuterium magic angle spinning NMR spectroscopy.

2H solid-state NMR experiments were performed under magic angle spinning on lipid bilayers oriented into nanotubes arrays, as a new method to assess the geometrical arrangement of the lipids. Orientational information is obtained from the intensities of the spinning sidebands. The lipid bilayers are formed by fusion of small unilamellar vesicles of DMPC-d54 inside a nanoporous anodic aluminum oxide, either by direct adsorption on the support or by tethering through a streptavidin/biotin linker. The results support that the quality of the lipid bilayers alignment is clearly in favor of the tethering rather than an adsorbed strategy.

Adsorption↗