15N chemical shift tensors and conformation of solid polypeptides containing 15N-labeled glycine residue by 15N NMR

Shoji, Akira; Ozaki, Takuo; Fujito, Teruaki; Deguchi, K.; Ando, Isao; Magoshi, Jun

doi:10.1016/s0022-2860(97)00258-5

Cited by 30 publications

(51 citation statements)

References 24 publications

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“…47 The collagen 15 N isotropic shift is 130 ppm, less downfield than poly(Lys-25) but still reflecting a turn conformation. 49 Further supporting the ␤-turn conformation of the central Pro-Gly residue pair is the Gly-3 15 N isotropic shift of 108.9 ppm, which is closer to the turn or coil value of 109.2 ppm than to either the helix (107.9 ppm) or sheet (109.7 ppm) isotropic shifts. The typical 13 C and 15 N line widths of poly(Lys-25) are 1.5-4 ppm and 8 -10 ppm, respectively.…”

Section: And 15 N Chemical Shift Anisotropymentioning

confidence: 83%

Structure of an elastin‐mimetic polypeptide by solid‐state NMR chemical shift analysis

et al. 2003

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The conformation of an elastin-mimetic recombinant protein, [(VPGVG)4(VPGKG)]39, is investigated using solid-state NMR spectroscopy. The protein is extensively labeled with 13C and 15N, and two-dimensional 13C-13C and 15N-13C correlation experiments were carried out to resolve and assign the isotropic chemical shifts of the various sites. The Pro 15N, 13Calpha, and 13Cbeta isotropic shifts, and the Gly-3 Calpha isotropic and anisotropic chemical shifts support the predominance of type-II beta-turn structure at the Pro-Gly pair but reject a type-I beta-turn. The Val-1 preceding Pro adopts mostly beta-sheet torsion angles, while the Val-4 chemical shifts are intermediate between those of helix and sheet. The protein exhibits a significant conformational distribution, shown by the broad line widths of the 15N and 13C spectra. The average chemical shifts of the solid protein are similar to the values in solution, suggesting that the low-hydration polypeptide maintains the same conformation as in solution. The ability to measure these conformational restraints by solid-state NMR opens the possibility of determining the detailed structure of this class of fibrous proteins through torsion angles and distances.

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Section: And 15 N Chemical Shift Anisotropymentioning

confidence: 83%

Structure of an elastin‐mimetic polypeptide by solid‐state NMR chemical shift analysis

et al. 2003

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“…31,[35][36][37][38][39][40][41][42] In addition, dipolar-dephased CPMAS spectra were also used for assigning 13 C resonances. Assignments of the 13 C peaks in the aliphatic region to different amino acid residues at concentration levels above 1% nmol in collgen are summarized in Figure 4.…”

Section: Isotropicmentioning

confidence: 99%

Solid‐state NMR studies of collagen‐based parchments and gelatin

Aliev

2005

Biopolymers

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Historical collagen-based parchments have been studied by solid-state NMR. In addition, new parchment (produced according to traditional methods) and gelatin from bovine skin were also studied. Wideline 1H and MAS 13C measurements were carried out directly on intact parchments. A simple approach is proposed for evaluation of the extent of parchment degradation based on the linewidth changes in the 13C CPMAS spectra relative to new parchment and gelatin. Structural (bound) water content was estimated from wideline 1H NMR lineshape and relaxation time measurements. It was found that the relative water content in parchments correlates linearly with 13C MAS linewidths. Its decrease on parchment degradation indicates that structural water molecules are of primary importance in stabilizing higher order collagen structures. Backbone and side chain dynamics of collagen in parchments were compared to those of gelatin based on the 13C dipolar-dephased experiments. Carbonyl 13C chemical shift anisotropies were measured to deduce the geometry of the collagen backbone motion. Unlike previous studies, we found that the collagen backbone motion is similar to that found in other proteins and occurs primarily via small-angle librations about internal bond directions.

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“…The 15 N and 13 C chemical shifts have been used as an analytical tool to determine polypeptide main chain conformations. 15,16,144,145 Important structural information such as the molecular orientation in space or the size of the dipolar coupling, however, are lost. Therefore, methods have been developed that selectively reintroduce the dipolar interaction term into magic angle spinning spectroscopy (reviewed in Refs.…”

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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15N chemical shift tensors and conformation of solid polypeptides containing 15N-labeled glycine residue by 15N NMR

Cited by 30 publications

References 24 publications

Structure of an elastin‐mimetic polypeptide by solid‐state NMR chemical shift analysis

Structure of an elastin‐mimetic polypeptide by solid‐state NMR chemical shift analysis

Solid‐state NMR studies of collagen‐based parchments and gelatin

Peptide structural analysis by solid-state NMR spectroscopy

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