In vivo fragment complementation of a (β/α)8 barrel protein: generation of variability by recombination
✍ Scribed by Xavier Soberón; Patricia Fuentes-Gallego; Gloria Saab-Rincón
- Book ID
- 117106275
- Publisher
- Elsevier Science
- Year
- 2004
- Tongue
- English
- Weight
- 424 KB
- Volume
- 560
- Category
- Article
- ISSN
- 0014-5793
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract The (β/α)~8~‐barrel is one of the most abundant folds found in enzymes. To identify the independent folding units and the segment(s) that correspond to a minimum core structure within a (β/α)~8~‐barrel protein, fragmentation experiments were performed with __Escherichia coli__ phosphori
Recombination in vivo was studied in recA- heterozygous lacZ merodiploids by performing beta-galactosidase assays after infection with lambda precA+. Recombination as measured by beta-galactosidase production was a linear function of lambda pecA+ multiplicity of infection (MOI) when the strain conta
## Abstract Many (α/β)~8~‐barrel enzymes contain their conserved sequence regions at or around the β‐strand segments that are often preceded and succeeded by glycines and prolines, respectively. α‐Amylase is one of these enzymes. Its sequences exhibit a very low degree of similarity, but strong con