Stability and activity modulation of chymotrypsins in AOT reversed micelles by protein-interface interaction : Interaction of alpha-chymotrypsin with a negative interface leads to a cooperative breakage of a salt bridge that keeps the catalytic active conformation (Ile16-Asp194) /
Đã lưu trong:
| Hovedforfatter: | Almeida, Fabio C. L. |
|---|---|
| Andre forfattere: | Chaimovich, Hernan., Valente, Ana Paula. |
| Format: | Bài viết |
| Sprog: | English |
| Fag: | |
| Tags: |
Tilføj Tag
Ingen Tags, Vær først til at tagge denne postø!
|
| Thư viện lưu trữ: | Thư viện Trường Đại học Đà Lạt |
|---|
Lignende værker
- Thermobarostability of alpha -chymotrypsin in reversed micelles of aerosol OT in octane solvated by water-glycerol mixtures /
-
Modeling of enzymatic reactions in vesicles : The case of alpha-chymotrypsin /
af: Blocher, Markus. - Kinetic characterization of penicillium citrinum lipase in AOT/lsooctane-reversed micelles /
-
Large acceleration of alpha-chymotrypsin-catalyzed dipeptide formation by 18-crown-6 in organic solvents /
af: Unen, Dirk-Jan van. - Deactivation and conformational changes of cutinase in reverse micelles /