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자연과학대학
화학·나노과학전공
Journal papers
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Rearrangement of tryptophan residues in caspase-3 active site upon activation
Title
Rearrangement of tryptophan residues in caspase-3 active site upon activation
Authors
Park I.-S.
;
Moon H.R.
;
Seok H.
;
Lee M.
Ewha Authors
이민영
SCOPUS Author ID
이민영
Issue Date
2004
Journal Title
Biochimica et Biophysica Acta - Proteins and Proteomics
ISSN
1570-9639
Citation
Biochimica et Biophysica Acta - Proteins and Proteomics vol. 1700, no. 1, pp. 5 - 9
Indexed
SCIE; SCOPUS
Document Type
Article
Abstract
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 cleavage. In addition, two mutant proteins that have only one tryptophan residue also showed the similar changes. These data indicate that the activation of caspase-3 resulted in the reorganization of both tryptophan residues. © 2004 Elsevier B.V. All rights reserved.
DOI
10.1016/j.bbapap.2004.03.008
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