Stability of wild-type and mutant RTEM-1 β-lactamases: Effect of the disulfide bond
✍ Scribed by Steve C. Schultz; Gloria Dalbadie-McFarland; James J. Neitzel; John H. Richards
- Publisher
- John Wiley and Sons
- Year
- 1987
- Tongue
- English
- Weight
- 958 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
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One of the best-studied examples of a class A beta-lactamase is Escherichia coli TEM-1 beta-lactamase. In this class of enzymes, the active-site serine residue takes on the role of a nucleophile and carries out beta-lactam hydrolysis. Here, the structures of the wild-type and the S70G enzyme determi
## Abstract __Cis__–__trans__ isomerization of amide bonds plays critical roles in protein molecular recognition, protein folding, protein misfolding, and disease. Aromatic–proline sequences are particularly prone to exhibit __cis__ amide bonds. The roles of residues adjacent to a tyrosine–proline