Origin of the Residual NMR Linewidth of a Peptide Bound to a Resin under Magic Angle Spinning

Elbayed, Karim; Bourdonneau, Maryse; Furrer, Julien; Richert, Thierry; Raya, Jésus; Hirschinger, Jérôme; Piotto, Martial

doi:10.1006/jmre.1998.1624

Cited by 34 publications

(37 citation statements)

References 15 publications

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“…MAS nmr spectroscopy therefore allows for the detailed analysis of the growing peptide chain and concomitantly the monitoring of the synthetic progress. [141][142][143] Magic angle spinning results in well-resolved nmr spectra in which sample homogeneity determines to a large extent the half width of the nmr resonances. The 15 N and 13 C chemical shifts have been used as an analytical tool to determine polypeptide main chain conformations.…”

Section: Mas Solid-state Nmr Spectroscopy On Synthetic Peptidesmentioning

confidence: 99%

Peptide structural analysis by solid-state NMR spectroscopy

et al. 1999

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Solid‐state nmr spectroscopy provides a robust method for investigating polypeptides that have been prepared by chemical synthesis and that are immobilized by strong interactions with solid surfaces or large macroscopic complexes. Solid‐state nmr spectroscopy has been widely used to investigate membrane polypeptides or peptide aggregates such as amyloid fibrils. Whereas magic angle spinning solid‐state nmr spectroscopy allows one to measure distances and dihedral angles with high accuracy, static membrane samples that are aligned with respect to the magnetic field direction allow one to determine the secondary structure of bound polypeptides and their orientation with respect to the bilayer normal. Peptide dynamics and the effect of polypeptides on the macroscopic phase preference of phospholipid membranes have been investigated in nonoriented samples. Investigations of the structure and topology of membrane channels, peptide antibiotics, signal sequences as well as model systems that allow one to dissect the interaction contributions in phospholipid membranes will be presented in greater detail. © 1999 John Wiley & Sons, Inc. Biopoly 51: 174–190, 1999

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Section: Mas Solid-state Nmr Spectroscopy On Synthetic Peptidesmentioning

confidence: 99%

Peptide structural analysis by solid-state NMR spectroscopy

et al. 1999

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“…A rapid inspection of the values indicates that the extreme narrowing conditions cannot be assumed, as was previously claimed in our previous paper. 18 In fact, the T 1 values are higher than the T 2 values, indicating, as stated previously with the proton, a relatively slow dynamic behavior. Contrary to proton, it is noteworthy that the contribution of transverse relaxation to the line broadening is not negligible for carbon.…”

Section: Dynamic Study Of the Tetrapeptide Ala-ile-gly-met In Solutiomentioning

confidence: 77%

“…The linewidth decreases when going from of 0 to 500 Hz and then remains constant up to a speed of 12 kHz. 3,18 It appears, therefore, that the solvent reintroduces enough mobility in the tetrapeptide to average out most of the dipolar and CSA interactions.…”

Section: Possible Causes Of Line Broadeningmentioning

confidence: 96%

“…In a recent study, we showed that most of the proton line broadening of the bound tetrapeptide Ala-Ile-Gly-Met was due to some incomplete averaging of magnetic susceptibility effects. 18 In this paper, we present a complete study of the mechanisms of line broadening that occur when the tetrapeptide Ala-Ile-Gly-Met is covalently bound to three different solid supports. Results obtained on the Wang, PEGA 19 and POEPOP 20 resins are presented.…”

Section: Introductionmentioning

confidence: 99%

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Dynamic and magnetic susceptibility effects on the MAS NMR linewidth of a tetrapeptide bound to different resins

Furrer

Elbayed

Bourdonneau

et al. 2001

Magnetic Reson in Chemistry

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Under magic angle spinning, the NMR spectrum of the tetrapeptide Ala-Ile-Gly-Met bound to a Wang resin, and swollen in DMF, exhibits proton and carbon linewidths that are sharp enough to allow the complete characterization of the peptide using classical liquid-state NMR methods. The proton linewidths of the bound peptide remain, however, about three times larger than those of the free peptide in solution. The residual NMR linewidth originates essentially from incompletely averaged magnetic susceptibility effects due to the Wang resin. Replacing the aromatic Wang resin with a PEGA or POEPOP resin removes this effect. To investigate the contribution to line broadening of the peptide dynamics, relaxation studies were performed on the peptide bound to Wang and POEPOP resins.

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“…Most of this effect can be span away by magic angle spinning already at moderate rates, and thus high-resolution magic angle spinning (HRMAS) can produce 1 H spectra that rival, in favorable cases, with liquid-state (ls) NMR ones. 4 This inclined to the introduction of standard ls-NMR procedures, such as extreme B 0 field homogeneity enhancement (high-order 'shimming') and built-in pulsed Ł Correspondence to: Stefano Caldarelli, JE 2421 TRACES Aix-Marseille Université, Campus Scientifique de Saint Jérôme F-13013 Marseille, France. E-mail: s.caldarelli@univ-cezanne.fr field gradient capabilities for coherent pathway selection and, accessorily, for molecular mobility studies.…”

Section: Introductionmentioning

confidence: 99%

Chromatographic NMR: a tool for the analysis of mixtures of small molecules

Caldarelli

2007

Magn. Reson. Chem.

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The addition of a solid to a mixture of small molecules introduces variations on the average translational mobility of these latter, proportional to the affinity of a given moiety for the less-mobile phase. This effect is at the basis of chromatographic separation, but can be used to simplify the NMR analysis of mixtures as well. In fact, as the induced differences in molecular mobility can span orders of magnitude, it becomes a much easier task to split the overall NMR spectrum of the mixture into one of the pure components using pulsed field gradient (PFG) methods. We have demonstrated recently this approach, in the context of HRMAS (high-resolution magic angle spinning) NMR, as required to recover high-resolution spectra in solid/liquid mixtures. In this review, we shall cover some of the principles and the practicality of this HRMAS-PFG approach for the study of mixtures. A comparison of the actual (in LC) and virtual (in NMR) separation capabilities of a few combinations of solid phase material/solvent composition shows similarities but also some striking differences: bare (not functionalized) silica expresses a superior potential for resolving spectral components than expected on the basis of the LC outcome.

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Origin of the Residual NMR Linewidth of a Peptide Bound to a Resin under Magic Angle Spinning

Cited by 34 publications

References 15 publications

Peptide structural analysis by solid-state NMR spectroscopy

Peptide structural analysis by solid-state NMR spectroscopy

Dynamic and magnetic susceptibility effects on the MAS NMR linewidth of a tetrapeptide bound to different resins

Chromatographic NMR: a tool for the analysis of mixtures of small molecules

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