✦ LIBER ✦

Magic-Angle Spinning Solid-State NMR Spectroscopy of the β1 Immunoglobulin Binding Domain of Protein G (GB1): 15 N and 13 C Chemical Shift Assignments and Conformational Analysis

✍ Scribed by Franks, W. Trent; Zhou, Donghua H.; Wylie, Benjamin J.; Money, Brian G.; Graesser, Daniel T.; Frericks, Heather L.; Sahota, Gurmukh; Rienstra, Chad M.

Book ID: 126434634
Publisher: American Chemical Society
Year: 2005
Tongue: English
Weight: 992 KB
Volume: 127
Category: Article
ISSN: 0002-7863
DOI: 10.1021/ja044497e

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Automated protein resonance assignments

Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of β1 immunoglobulin binding domain of protein G (GB1)

✍ Hunter N. B. Moseley; Lindsay J. Sperling; Chad M. Rienstra 📂 Article 📅 2010 🏛 Springer Netherlands 🌐 English ⚖ 346 KB

13C and15N chemical shift assignments an

13C and15N chemical shift assignments and secondary structure of the B3 immunoglobulin-binding domain of streptococcal protein G by magic-angle spinning solid-state NMR spectroscopy

✍ Philippe S. Nadaud; Jonathan J. Helmus; Christopher P. Jaroniec 📂 Article 📅 2007 🏛 Springer-Verlag 🌐 English ⚖ 385 KB

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