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Evidences for the unfolding mechanism of three‐dimensional domain swapping
Author(s) -
Liu Zhirong,
Huang Yongqi
Publication year - 2013
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2209
Subject(s) - domain (mathematical analysis) , folding (dsp implementation) , protein folding , chemistry , mutant , biophysics , mechanism (biology) , kinetics , protein domain , thioredoxin , crystallography , computational biology , physics , biology , biochemistry , enzyme , mathematics , mathematical analysis , electrical engineering , quantum mechanics , engineering , gene
The full or partial unfolding of proteins is widely believed to play an essential role in three‐dimensional domain swapping. However, there is little research that has rigorously evaluated the association between domain swapping and protein folding/unfolding. Here, we examined a kinetic model in which domain swapping occurred via the denatured state produced by the complete unfolding of proteins. The relationships between swapping kinetics and folding/unfolding thermodynamics were established, which were further adopted as criteria to show that the proposed mechanism dominates in three representative proteins: Cyanovirin‐N (CV‐N), the C‐terminal domain of SARS‐CoV main protease (M pro ‐C), and a single mutant of oxidized thioredoxin (Trx_W28A ox ).