Reassessment of the catalytic activity and substrate specificity of fkbp35 from plasmodium knowlesi using protease-free assay
FK506-binding protein35 of Plasmodium knowlesi (Pk-FKBP35) is a member of peptidyl prolyl cis-trans isomerase (PPIase) and is considered as a promising avenue of antimalarial drug target development. This protein is organized into the N-terminal domain responsible for PPIase catalytic activity follo...
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| Main Authors: | , , , , |
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| Format: | Article |
| Published: |
Universiti Malaysia Sabah
2020
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| Online Access: | http://psasir.upm.edu.my/id/eprint/87406/ https://jurcon.ums.edu.my/ojums/index.php/bijb/index |
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| Institution: | Universiti Putra Malaysia |