Bacteriophage P22 scaffolding protein forms oligomers in solution
โ Scribed by Matthew H. Parker; Walter F. Stafford III; Peter E. Prevelige Jr
- Book ID
- 115627904
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 302 KB
- Volume
- 268
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
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 ห-protons indicates that the N-terminal half of this
Spontaneous mutants of S. typhimUrium resistant to thiolutin are conditionally non-permissive for phage P22 development (Joshi and Chakravorty 1979). At 40 ยฐ C non-infective phage particles are produced. Phage development in two nonpermissive hosts (18/MC4 and 153/MC4) has been studied in detail. Th