AI Article Synopsis
- The study characterized the active site of the apoptotic enzyme caspase-3 by examining the intrinsic fluorescence of two tryptophan residues.
- The researchers looked at how temperature affected the fluorescence, analyzed energy transfer between the tryptophan residues, and measured fluorescence quenching caused by tetrapeptide inhibitors.
- They found that the fluorescence lifetimes of caspase-3 decreased significantly when it interacted with inhibitors, indicating an electron transfer process was occurring.
Article Abstract
The active site of an apoptotic enzyme caspase-3 was characterized by measuring the intrinsic fluorescence of two tryptophan residues. Temperature dependence of the intrinsic fluorescence, the energy homotransfer between the tryptophan residues, and the fluorescence quenching by tetrapeptide inhibitors were investigated by the fluorescence lifetime measurements. It has been observed that the fluorescence lifetimes of caspase-3 in complex with inhibitors were significantly shortened by the electron transfer process.
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| http://dx.doi.org/10.1016/s0167-4838(02)00333-3 | DOI Listing |
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