𝔖 Bobbio Scriptorium
✦   LIBER   ✦

A Minimal Transmembrane β-Barrel Platform Protein Studied by Nuclear Magnetic Resonance †,‡

✍ Scribed by Johansson, Maria U.; Alioth, Simon; Hu, Kaifeng; Walser, Reto; Koebnik, Ralf; Pervushin, Konstantin


Book ID
127032675
Publisher
American Chemical Society
Year
2007
Tongue
English
Weight
855 KB
Volume
46
Category
Article
ISSN
0006-2960

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


Microheterogeneity of bovine myelin basi
✍ Charles M. Deber; Sela Cheifetz; Mario A. Moscarello 📂 Article 📅 1983 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 228 KB 👁 2 views

## Synopsis Myelin basic protein isolated from bovine white matter is known to consist of a mixture of three or more "charge isomers," which can be separated by cation-exchange chromatography. We are using 360-MHz 'H-nmr spectroscopy to establish the chemical and structural differences among them.

The use of p-fluorobenzenesulfonyl chlor
✍ Ta-Hsiu Liao; K.Darrell Berlin 📂 Article 📅 1985 🏛 Elsevier Science 🌐 English ⚖ 890 KB

The reagent pfluorobenzenesulfonyl chloride modifies the protein side chains of tyrosine, lysine, and histidine and the a-NH2 group. The pfluorobenzenesulfonyl (Fbs-) group, identified by the 19F nuclear magnetic resonance signal, exhibits a different 19F chemical shift for each functional group mod