𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles

✍ Scribed by Christian Hilty; César Fernández; Gerhard Wider; Kurt Wüthrich

Book ID
110393575
Publisher
Springer Netherlands
Year
2002
Tongue
English
Weight
253 KB
Volume
23
Category
Article
ISSN
0925-2738

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Two-Dimensional NMR Experiments for the
Two-Dimensional NMR Experiments for the Assignment of Aromatic Side Chains in13C-labeled Proteins
✍ Jeanine J. Prompers; Anneke Groenewegen; Cornelis W. Hilbers; Henri A.M. Peperma 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 231 KB

As aromatic residues very often are part of the hydrophobic essential for an accurate and precise structure determination. core of proteins, the unambiguous assignment of the aromatic Therefore, methods for the unambiguous assignment of aroproton resonances is essential for an accurate and precise s

Novel Pulse Sequences for the Resonance
Novel Pulse Sequences for the Resonance Assignment of Aromatic Side Chains in13C-Labeled Proteins
✍ Frank Löhr; Heinz Rüterjans 📂 Article 📅 1996 🏛 Elsevier Science 🌐 English ⚖ 456 KB

Complete resonance assignments are mandatory for de-will refer to as (HB)CB(CG)CDHD. Finally, the assigned side-chain resonances are linked to the backbone by use of tailed NMR studies of protein structures in solution. In many proteins, aromatic residues are involved in the construction an (H)CCH-C