Rearrangement of tryptophan residues in caspase-3 active site upon activation.

Abstract excerpt

Caspase-3, one of the major apoptotic proteins, is a cysteine protease and exists as an inactive zymogen in healthy cells. In this study, the dynamic nature of the rearrangements of two tryptophan residues (Trp 206 and Trp 214) in the active sites of caspase-3 during the activation was analyzed by measuring the fluorescence lifetimes. Significant changes in the lifetime occurred upon activation by the specific...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Binding Sites
• Share to Caspase 3
• Share to Caspases