✦ LIBER ✦

19F and 13C NMR Signal Assignment and Analysis in a Perfluorinated Ionomer (Nafion) by Two-Dimensional Solid-State NMR

✍ Scribed by Chen, Q.; Schmidt-Rohr, K.

Book ID: 115533976
Publisher: American Chemical Society
Year: 2004
Tongue: English
Weight: 230 KB
Volume: 37
Category: Article
ISSN: 0024-9297
DOI: 10.1021/ma049759b

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Backbone Dynamics of the Nafion Ionomer

Backbone Dynamics of the Nafion Ionomer Studied by 19F-13C Solid-State NMR

✍ Qiang Chen; Klaus Schmidt-Rohr 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 500 KB

## Abstract The chain dynamics of a perfluorinated ionomer, Nafion®, have been studied by ^19^F and ^19^F‐^13^C solid‐state NMR at 295 K. The backbone of Nafion is essentially poly(tetrafluoroethylene) (PTFE), which was investigated for reference. Fast uniaxial rotations of the helical backbone wer

Structural Analysis of a Perfluorosulfon

Structural Analysis of a Perfluorosulfonate Ionomer in Solution by 19 F and 13 C NMR

✍ Takasaki, Mari; Kimura, Kazuo; Kawaguchi, Ken; Abe, Akira; Katagiri, Gen 📂 Article 📅 2005 🏛 American Chemical Society 🌐 English ⚖ 190 KB

Determination of Multiple φ-Torsion Angl

Determination of Multiple φ-Torsion Angles in Proteins by Selective and Extensive 13C Labeling and Two-Dimensional Solid-State NMR

✍ Mei Hong 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 198 KB

We describe an approach to efficiently determine the backbone conformation of solid proteins that utilizes selective and extensive (13)C labeling in conjunction with two-dimensional magic-angle-spinning NMR. The selective (13)C labeling approach aims to reduce line broadening and other multispin com

Signal assignments and chemical-shift st

Signal assignments and chemical-shift structural analysis of uniformly13C,15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under magic-angle spinning

✍ Toshimichi Fujiwara; Yasuto Todokoro; Hajime Yanagishita; Midori Tawarayama; Tos 📂 Article 📅 2004 🏛 Springer Netherlands 🌐 English ⚖ 518 KB

Assignment of the Nonexchanging Protons

Assignment of the Nonexchanging Protons of the α-Spectrin SH3 Domain by Two- and Three- Dimensional 1H–13C Solid-State Magic-Angle Spinning NMR and Comparison of Solution and Solid-State Proton Chemical Shifts

✍ Barth-Jan van Rossum; Federica Castellani; Kristina Rehbein; Jutta Pauli; Hartmu 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 215 KB 👁 1 views

The assignment of nonexchanging protons of a small microcrystalline protein, the alpha-spectrin SH3 domain (7.2 kDa, 62 residues), was achieved by means of three-dimensional (3D) heteronuclear (1H-13C-13C) magic-angle spinning (MAS) NMR dipolar correlation spectroscopy. With the favorable combinatio

η5-Cyclopentadienyl derivatives of tin(I

η5-Cyclopentadienyl derivatives of tin(II) studied by two-dimensional multinuclear magnetic resonance in solution and by 13C and 119Sn CP/MAS NMR in the solid state

✍ Bernd Wrackmeyer; Ēriks Kupče; Gerald Kehr; Angelika Sebald 📂 Article 📅 1992 🏛 John Wiley and Sons 🌐 English ⚖ 422 KB

## Abstract Absolute coupling signs of ^1^__J__(^119^Sn, ^13^C) (2__J__(^119^Sn, ^1^H) (n^5^‐C~5~H~5~)~2~Sn (1) and ^1^__J__(^119^Sn, ^13^C) (2__J__(^119^Sn, ^13^C) (3__J__(^119^Sn, ^1^H) (>O) in (__n__^5^‐C~5~Me~5~)~2~Sn (2) were determined using advanced direct and indirect two‐dimensional method