A practical guide for the setup of a 1H–31P–13C double cross-polarization (DCP) experiment

Ciesielski, W.; Kassassir, Hassan; Potrzebowski, Marek J.

doi:10.1016/j.ssnmr.2010.12.001

Cited by 3 publications

(4 citation statements)

References 35 publications

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“…The 1 H → 31 P– 13 C double cross-polarization (DCP) experiment was conducted on dry caddisfly silk with a 3.2 mm Varian triple resonance MAS probe. , The sample was spun at a slow speed (5 kHz MAS) to favor the zero-quantum transition during the second polarization transfer step . The highly sensitive DCP conditions were carefully calibrated using crystalline L-O-phosphoserine (Sigma Aldrich).…”

Section: Materials and Methodsmentioning

confidence: 99%

“…32,33 The sample was spun at a slow speed (5 kHz MAS) to favor the zero-quantum transition during the second polarization transfer step. 34 The highly sensitive DCP conditions were carefully calibrated using crystalline L-O-phosphoserine (Sigma Aldrich). The experimental parameters for the initial 1 H → 31 P CP step were a 3 μs 1 H π/2 pulse, a 1 ms ramped 1 H spin-lock pulse centered at 80 kHz radio frequency (rf) field strength, and a 31 P square contact pulse matched to the −1 spinning sideband of the Hartmann− Hahn profile.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

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β-Sheet Nanocrystalline Domains Formed from Phosphorylated Serine-Rich Motifs in Caddisfly Larval Silk: A Solid State NMR and XRD Study

et al. 2013

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Adhesive silks spun by aquatic caddisfly (order Trichoptera) larvae are used to build both intricate protective shelters and food harvesting nets underwater. In this study, we use 13C and 31P solid-state Nuclear Magnetic Resonance (NMR) and Wide Angle X-ray Diffraction (WAXD) as tools to elucidate molecular protein structure of caddisfly larval silk from the species Hesperophylax consimilis. Caddisfly larval silk is a fibroin protein based biopolymer containing mostly repetitive amino acid motifs. NMR and X-ray results provide strong supporting evidence for a structural model in which phosphorylated serine repeats (pSX)4 complex with divalent cations Ca2+ and Mg2+ to form rigid nanocrystalline β-sheet structures in caddisfly silk. 13C NMR data suggests that both phosphorylated serine and neighboring valine residues exist in a β-sheet secondary structure conformation while glycine and leucine residues common in GGX repeats likely reside in random coil conformations. Additionally, 31P chemical shift anisotropy (CSA) analysis indicates that the phosphates on phosphoserine residues are doubly ionized, and are charge-stabilized by divalent cations. Positively charged arginine side chains also likely play a role in charge stabilization. Finally, WAXD results finds that the silk is at least 7–8% crystalline, with β-sheet inter-plane spacings of 3.7 and 4.5 Å.

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Section: Materials and Methodsmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

β-Sheet Nanocrystalline Domains Formed from Phosphorylated Serine-Rich Motifs in Caddisfly Larval Silk: A Solid State NMR and XRD Study

et al. 2013

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“…Looking for further evidence that better defines the mechanism of thermal cyclization, we carried out 1 H– 13 C– 15 N double cross-polarization (DCP) experiment employing methodology discussed in our previous paper . We assumed that for Y*A DKP and YA* DKP samples (intermolecular process b′ ), the amide nitrogens will correlate only with directly bonded aliphatic carbons.…”

Section: Results and Discussionmentioning

confidence: 99%

“…Looking for further evidence that better defines the mechanism of thermal cyclization, we carried out employing methodology discussed in our previous paper. 37 We assumed that for Y*A DKP and YA* DKP samples (intermolecular process b′), the amide nitrogens will correlate only with directly bonded aliphatic carbons. In the case of intramolecular cyclization (also pathway b″) the amide nitrogens will be correlated with carbonyl carbons and adjacent Cα carbons.…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

Study of the Mechanism of Thermal Chemical Processes in the Crystals of YAF Tripeptides by Means of Mass Spectrometry and Solid State NMR

et al. 2013

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Thermal reactions in two Tyr-Ala-Phe (YAF) tripeptide crystals with different molecular packing (monoclinic and hexagonal), distinct stereochemistry of central amino acid (D or L alanine) and specific arrangement of molecules in the crystal lattice (head-to-tail) were investigated. Samples were heated up to 180 °C, while the melting point for YAF crystals is above the 220 °C. Below the melting temperature, in both cases the chemical reactions leading to formation of cyclic dipeptides (YA diketopiperazine) and leaving of phenylalanine were observed. Two possible mechanisms of chemical reaction in the crystal lattice assuming intra- and/or intermolecular pathways were considered. (13)C and (15)N enriched YAF samples were employed to study of mechanism of solid state reactivity using mass spectrometry and advanced solid state NMR techniques (2D DARR (Dipolar Assisted Rotational Resonance) and 2D Double CP (Cross-Polarization) correlations).

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Bandwidth in double cross-polarization MAS NMR spectroscopy

Tzou

2012

Solid State Nuclear Magnetic Resonance

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A practical guide for the setup of a 1H–31P–13C double cross-polarization (DCP) experiment

Cited by 3 publications

References 35 publications

β-Sheet Nanocrystalline Domains Formed from Phosphorylated Serine-Rich Motifs in Caddisfly Larval Silk: A Solid State NMR and XRD Study

β-Sheet Nanocrystalline Domains Formed from Phosphorylated Serine-Rich Motifs in Caddisfly Larval Silk: A Solid State NMR and XRD Study

Study of the Mechanism of Thermal Chemical Processes in the Crystals of YAF Tripeptides by Means of Mass Spectrometry and Solid State NMR

Bandwidth in double cross-polarization MAS NMR spectroscopy

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