𝔖 Bobbio Scriptorium
✦   LIBER   ✦

1H and 15N chemical shift assignments of a carboxy-terminal functional domain of the bacteriophage P22 scaffolding protein

✍ Scribed by Yahong Sun; N. Rama Krishna


Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
55 KB
Volume
37
Category
Article
ISSN
0749-1581

No coin nor oath required. For personal study only.

✦ Synopsis


The 15 N-labeled C-terminal functional domain of the bacteriophage P22 scaffolding protein was expressed and purified. The NMR chemical-shift assignments of this functional domain were determined. An analysis of the chemical shift indices for the ˛-protons indicates that the N-terminal half of this protein is unstructured whereas the C-terminal half is defined by a helix-loop-helix motif. Copyright


📜 SIMILAR VOLUMES


Characterisation of uniformly 13C, 15N l
✍ Tatiana Egorova-Zachernyuk; Barth van Rossum; Cees Erkelens; Huub de Groot 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 English ⚖ 306 KB

## Abstract In this investigation we report a complete assignment of ^13^C, ^1^H and ^15^N solution and solid state chemical shifts of two bacterial photosynthetic pigments, bacteriochlorophyll (BChl) __a__ and bacteriopheophytin (BPheo) __a__. Uniform stable‐isotope labelling strategies were devel

NMR chemical shift mapping of the bindin
✍ Jikui Song; John L. Markley 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 201 KB

## Abstract The substrate‐like inhibition of serine proteinases by avian ovomucoid domains has provided an excellent model for protein inhibitor‐proteinase interactions of the standard type. ^1^H,^15^N and ^13^C NMR studies have been undertaken on complexes formed between turkey ovomucoid third dom