## 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
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
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✦ 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
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## 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