Canonical loops of protein inhibitors of serine proteinases occur in proteins having completely different folds. In this article, conformations of the loops have been analyzed for inhibitors belonging to 10 structurally different families. Using deviation in Calpha-Calpha distances as a criterion fo
✦ LIBER ✦
Protein Inhibitors of Serine Proteinases: Role of Backbone Structure and Dynamics in Controlling the Hydrolysis Constant ‡
✍ Scribed by Song, Jikui; Markley, John L.
- Book ID
- 127163880
- Publisher
- American Chemical Society
- Year
- 2003
- Tongue
- English
- Weight
- 159 KB
- Volume
- 42
- Category
- Article
- ISSN
- 0006-2960
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## Abstract The effect of structural dynamics on enzyme activity and thermostability has thus far only been investigated in detail for the serine protease α‐chymotrypsin (for a recent review see Solá et al., Cell Mol Life Sci 2007, 64(16): 2133–2152). Herein, we extend this type of study to a struc
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